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Grünewald, Jan, and Mohamed A. Marahiel. "Chemoenzymatic and Template-Directed Synthesis of Bioactive Macrocyclic Peptides." Microbiology and Molecular Biology Reviews 70, no. 1 (March 2006): 121–46. http://dx.doi.org/10.1128/mmbr.70.1.121-146.2006.
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SUMMARY Non-ribosomally synthesized peptides have compelling biological activities ranging from antimicrobial to immunosuppressive and from cytostatic to antitumor. The broad spectrum of applications in modern medicine is reflected in the great structural diversity of these natural products. They contain unique building blocks, such as d-amino acids, fatty acids, sugar moieties, and heterocyclic elements, as well as halogenated, methylated, and formylated residues. In the past decades, significant progress has been made toward the understanding of the biosynthesis of these secondary metabolites by nonribosomal peptide synthetases (NRPSs) and their associated tailoring enzymes. Guided by this knowledge, researchers genetically redesigned the NRPS template to synthesize new peptide products. Moreover, chemoenzymatic strategies were developed to rationally engineer nonribosomal peptides products in order to increase or alter their bioactivities. Specifically, chemical synthesis combined with peptide cyclization mediated by nonribosomal thioesterase domains enabled the synthesis of glycosylated cyclopeptides, inhibitors of integrin receptors, peptide/polyketide hybrids, lipopeptide antibiotics, and streptogramin B antibiotics. In addition to the synthetic potential of these cyclization catalysts, which is the main focus of this review, different enzymes for tailoring of peptide scaffolds as well as the manipulation of carrier proteins with reporter-labeled coenzyme A analogs are discussed.
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Khaldi, Nora. "Bioinformatics approaches for identifying new therapeutic bioactive peptides in food." Functional Foods in Health and Disease 2, no. 10 (October 15, 2012): 325. http://dx.doi.org/10.31989/ffhd.v2i10.80.
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The traditional methods for mining foods for bioactive peptides are tedious and long. Similar to the drug industry, the length of time to identify and deliver a commercial health ingredient that reduces disease symptoms can take anything between 5 to 10 years. Reducing this time and effort is crucial in order to create new commercially viable products with clear and important health benefits. In the past few years, bioinformatics, the science that brings together fast computational biology, and efficient genome mining, is appearing as the long awaited solution to this problem. By quickly mining food genomes for characteristics of certain food therapeutic ingredients, researchers can potentially find new ones in a matter of a few weeks. Yet, surprisingly, very little success has been achieved so far using bioinformatics in mining for food bioactives. The absence of food specific bioinformatic mining tools, the slow integration of both experimental mining and bioinformatics, and the important difference between different experimental platforms are some of the reasons for the slow progress of bioinformatics in the field of functional food and more specifically in bioactive peptide discovery. In this paper I discuss some methods that could be easily translated, using a rational peptide bioinformatics design, to food bioactive peptide mining. I highlight the need for an integrated food peptide database. I also discuss how to better integrate experimental work with bioinformatics in order to improve the mining of food for bioactive peptides, therefore achieving a higher success rates.Keywords: bioactive peptides, bioinformatics, mining food, therapeutic properties, food proteins, functional food.
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Hayes, Maria. "Bioactive Peptides in Preventative Healthcare: An Overview of Bioactivities and Suggested Methods to Assess Potential Applications." Current Pharmaceutical Design 27, no. 11 (April 27, 2021): 1332–41. http://dx.doi.org/10.2174/1381612827666210125155048.
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Food derived bioactive peptides can be generated from various protein sources and usually consist of between 2-30 amino acids with bulky, side-chain aromatic amino acids preferred in the ultimate and penultimate positions at the C-terminal end of the amino acid chain. They are reported to impart a myriad of preventative health beneficial effects to the consumer once ingested and these include heart health benefits through inhibition of enzymes including renin (EC 3.4.23.15) and angiotensin- I-converting enzyme (ACE-1; EC 3.4.15.1) within the renin angiotensin aldosterone system (RAAS) anti-inflammatory (due to inhibition of ACE-I and other enzymes) and anti-cancer benefits, prevention of type-2 diabetes through inhibition of dipeptidyl peptidase IV (DPP-IV), bone and dental strength, antimicrobial and immunomodulatory effects and several others. Peptides have also reported health benefits in the treatment of asthma, neuropathic pain, HIV and wound healing. However, the structure, amino acid composition and length of these peptides, along with the quantity of peptide that can pass through the gastrointestinal tract and often the blood-brain barrier (BBB), intact and reach the target organ, are important for the realisation of these health effects in an in vivo setting. This paper aims to collate recent important research concerning the generation and detection of peptides in the laboratory. It discusses products currently available as preventative healthcare peptide options and relevant legislation barriers to place a food peptide product on the market. The review also highlights useful in silico computer- based methods and analysis that may be used to generate specific peptide sequences from proteins whose amino acid sequences are known and also to determine if the peptides generated are unique and bioactive. The topic of food-derived bioactive peptides for health is of great interest to scientific research and industry due to evolving drivers in food product innovation, including health and wellness for the elderly, infant nutrition and optimum nutrition for sports athletes and the humanisation of pets. This paper provides an overview of what is required to generate bioactive peptide containing hydrolysates, what methods should be used in order to characterise the beneficial health effects of these hydrolysates and the active peptide sequences, potential applications of bioactive peptides and legislative requirements in Europe and the United States. It also highlights success stories and barriers to the development of peptide-containing food products that currently exist.
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Hidayah, Nur, and Sandy Ardiansyah. "The Potential of Bioactive Peptides from Animal Protein Sources as a Mental Health Problems Prevention." AGRITROPICA : Journal of Agricultural Sciences 4, no. 2 (December 28, 2021): 114–21. http://dx.doi.org/10.31186/j.agritropica.4.2.114-121.
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Protein is one of the substances of nutrition macro that is needed by the body are known to contain bioactive peptides. Protein sources can be from vegetables and animals, based on research an animal protein sources more complete, balanced, easily digested and absorbed than vegetable protein sources. Some sources of animal protein (milk, eggs, meat, and products derived and processed) were reported that contain of bioactive peptides. Bioactive peptide has effect as antimicrobial, antithrombotic, antihypertensive, opioid, immunomodulatory, binder minerals, antioxidants, and prevent mental health disorder. The purpose of this paper is to review the peptide bioactive, relationship of mental health with peptide bioactive, and prevention of mental helath problems with bioactive peptide from animal protein sources. Peptides bioactive is an organic substance that is formed by amino acids (2-30 pieces) with the bond of the peptide and the weight of the molecule is small (unit Dalton). Mental health is the condition of the welfare (well-being) of an individual that is aware of its ability to own, can cope with the pressure of life which is normal, can work in a productive and can give a contribution to the community. Peptides bioactive shows such as opioids and inhibit the activity of the enzyme prolyl endopeptidase (PEP, EC 3.4.21.26) that play a role important in the treatment of disorders of the mind because work on the system nerve central (CNS) and can give the effect of a positive on motivation, behavior, stress, control the intake of food or the perception of the sense of pain. Some proteins of animal that has been proven to be able to prevent mental health problems namely, bovine, yogurt, and fresh milk. Still a lot of opportunities in the business of exploration of the source of the protein animal in producing the product peptide bioactive for commercial.
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Nurdiani, Rahmi, Todor Vasiljevic, Tanoj K. Singh, Osaana N. Donkor, Asep A. Prihanto, and Titis S. Kusuma. "Stability of an anticancer peptide isolated from Flathead by-products during in vitro gastrointestinal digestion." Functional Foods in Health and Disease 12, no. 4 (April 29, 2022): 198. http://dx.doi.org/10.31989/ffhd.v12i4.904.
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Background: Several peptides from seafood have shown effective anticancer activities. Nonetheless, one of the most significant challenges in developing fish peptides as functional food ingredients is proving their efficacy as anticancer agents. This study was aimed to evaluate the anticancer capacity and stability of a purified peptide (H. Met-Gly-Pro-Pro-Gly-Leu-Ala-Gly-Ala-Pro-Gly-Glu-Ala-Gly-Arg.OH) during a simulated gastrointestinal (GI) digestion.Methods: The anticancer activity of the peptide(s) before, during, and after GI digestion was analyzed against colon cancer cells (HT-29). Changes in cell morphology were assessed using an inverted microscope, while the degree of apoptosis was observed using a Muse Cell Analyzer.Results: Results showed little or no hydrolysis of the bioactive peptide by pepsin was observed, indicating the peptide was resistant to digestion in gastric conditions. The growth of HT-29 cells was significantly inhibited (P < 0.05) by the un-digested peptide and peptide(s) present in the digesta that was yielded by gastric and gastrointestinal digestion up to 28.89%, 29.68%, and 38.3%, respectively. HT-29 cells treated with pepsin and pancreatin digested peptides showed the highest cell death (3.54±2.30%).Conclusion: Overall, the findings showed that the purified peptide has the potency to be used in cancer therapy via oral administration and/or incorporation in food(s) applications for the treatment of specific cancer.Keywords: bioactive peptide; digestion; fish by-products; hydrolysis
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Chelliah, Ramachandran, Shuai Wei, Eric Banan-Mwine Daliri, Fazle Elahi, Su-Jung Yeon, Akanksha Tyagi, Shucheng Liu, Inamul Hasan Madar, Ghazala Sultan, and Deog-Hwan Oh. "The Role of Bioactive Peptides in Diabetes and Obesity." Foods 10, no. 9 (September 18, 2021): 2220. http://dx.doi.org/10.3390/foods10092220.
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Bioactive peptides are present in most soy products and eggs and have essential protective functions. Infection is a core feature of innate immunity that affects blood pressure and the glucose level, and ageing can be delayed by killing senescent cells. Food also encrypts bioactive peptides and protein sequences produced through proteolysis or food processing. Unique food protein fragments can improve human health and avoid metabolic diseases, inflammation, hypertension, obesity, and diabetes mellitus. This review focuses on drug targets and fundamental mechanisms of bioactive peptides on metabolic syndromes, namely obesity and type 2 diabetes, to provide new ideas and knowledge on the ability of bioactive peptide to control metabolic syndromes.
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Li, Xiangyang, Manli Guo, Jingtian Chi, and Jiangang Ma. "Bioactive Peptides from Walnut Residue Protein." Molecules 25, no. 6 (March 12, 2020): 1285. http://dx.doi.org/10.3390/molecules25061285.
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Walnut residue is a kind of high-quality plant protein resource. The bioactive peptide prepared from walnut residue has excellent health care functions such as antioxidation and antihypertensive activity, but at present, walnut residue is often regarded as waste or low value feed, fertilizer and other materials. The uneconomical use of walnut residue has hindered the development of the walnut industry to some extent. Effective utilization of walnut residue protein to develop bioactive peptides and other products is of great significance to realize the comprehensive utilization of walnut residue, improve the added value of by-products, and change the current low utilization rate of walnut residue. In this paper, the preparation, purification and structure identification of walnut protein bioactive peptides are reviewed, and different functional walnut active peptides (WBPs) are introduced. The potential effects of these bioactivities on human health and their different uses in food, medicine and other industries are discussed. The purpose is to provide reference information for the effective utilization of walnut residue resources and the development of walnut industry.
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Aluko, Rotimi E. "Determination of Nutritional and Bioactive Properties of Peptides in Enzymatic Pea, Chickpea, and Mung Bean Protein Hydrolysates." Journal of AOAC INTERNATIONAL 91, no. 4 (July 1, 2008): 947–56. http://dx.doi.org/10.1093/jaoac/91.4.947.
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Abstract Within the primary structure of many pea and mung bean proteins are peptide sequences that can potentially be used in the formulation of therapeutic products for the treatment and prevention of human diseases. However, these peptide sequences need protease treatments before they can be released free of the parent proteins. Unlike chemical hydrolysis, enzymatic treatment enables more efficient tailoring of peptide products without formation of toxic by-products or destruction of amino acids. This review provides information on current methods that have been used to convert inactive pea and mung bean proteins into bioactive peptides. It focuses on 3 main bioactive properties, such as inhibitions of (1) angiotensin converting enzyme (ACE) activity; (2) calmodulin (CaM)-dependent enzymes; and (3) copper-chelating activity. ACE is an established marker for hypertension, high levels of some CaM-dependent enzymes are risk factors for various human diseases including cancer and Alzheimer's disease, and high vascular copper concentrations may potentiate atherosclerosis. Also reviewed are the production and evaluation of activity of hypoallergenic peptides that may offer protection against anaphylactic reactions. The 3 main proteins discussed are chickpea, mung bean, and field pea.
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Hubrich, Florian, Alessandro Lotti, Thomas A. Scott, and Jörn Piel. "Uncovering Novel Peptide Chemistry from Bacterial Natural Products." CHIMIA International Journal for Chemistry 75, no. 6 (June 30, 2021): 543–47. http://dx.doi.org/10.2533/chimia.2021.543.
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Nature has evolved a remarkable array of biosynthetic enzymes that install diverse chemistries into natural products (NPs), bestowing them with a range of important biological properties that are of considerable therapeutic value. This is epitomized by the ribosomally synthesized and post-translationally modified peptides (RiPPs), a class of peptide natural products that undergo extensive post-translational modifications to produce structurally diverse bioactive peptides. In this review, we provide an overview of our research into the proteusin RiPP family, describing characterized members and the maturation enzymes responsible for their unique chemical structures and biological activities. The diverse enzymology identified in the first two proteusin pathways highlights the enormous potential of the RiPP class for new lead structures and novel pharmacophore-installing maturases as biocatalytic tools for drug discovery efforts.
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Caliceti, C., A. L. Capriotti, D. Calabria, F. Bonvicini, R. Zenezini Chiozzi, C. M. Montone, S. Piovesana, et al. "Peptides from Cauliflower By-Products, Obtained by an Efficient, Ecosustainable, and Semi-Industrial Method, Exert Protective Effects on Endothelial Function." Oxidative Medicine and Cellular Longevity 2019 (February 6, 2019): 1–13. http://dx.doi.org/10.1155/2019/1046504.
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The large amount of cauliflower industry waste represents an unexplored source of bioactive compounds. In this work, peptide hydrolysates from cauliflower leaves were characterized by combined bioanalytical approaches. Twelve peptide fractions were studied to evaluate unexplored biological activities by effect-based cellular bioassays. A potent inhibition of intracellular xanthine oxidase activity was observed in human vascular endothelial cells treated with one fraction, with an IC50 = 8.3±0.6 μg/ml. A different fraction significantly induced the antioxidant enzyme superoxide dismutase 1 and decreased the tumor necrosis factor α-induced VCAM-1 expression, thus leading to a significant improvement in the viability of human vascular endothelial cells. Shotgun peptidomics and bioinformatics were used to retrieve the most probable bioactive peptide sequences. Our study shows that peptides from cauliflower waste should be recycled for producing valuable products useful for the prevention of endothelial dysfunction linked to atherogenesis progression.
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Calcott, Mark J., and David F. Ackerley. "Genetic manipulation of non-ribosomal peptide synthetases to generate novel bioactive peptide products." Biotechnology Letters 36, no. 12 (September 12, 2014): 2407–16. http://dx.doi.org/10.1007/s10529-014-1642-y.
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Kitts, David D. "Bioactive substances in food: identification and potential uses." Canadian Journal of Physiology and Pharmacology 72, no. 4 (April 1, 1994): 423–34. http://dx.doi.org/10.1139/y94-062.
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Bioactive substances in foods can represent "extranutritional" constituents naturally present in small quantities in the food matrix, produced upon either in vivo or industrial enzymatic digestion, the latter being a result of food-processing activities. Bioactive constituents of food evoke physiological, behavioral, and immunological effects. Evidence from both epidemiological and animal studies has suggested chemopreventative roles for phytochemicals in certain forms of cancers and in the control of hyperlipidemia. Secondary products of plant metabolism can modulate xenobiotic metabolizing and cholesterol synthetic enzymes. Unique physicochemical properties of food-derived peptides with characteristic amino acid composition and sequences have been reported to influence intestinal transit, modify nutrient absorption and excretion, and exhibit immuno-stimulating and antihypertensive activity. Biologically active peptides derived from casein, fish muscle, and plant protein hydrolysates have been isolated, purified, and identified in peptide sequence studies. Therapeutic proteins (e.g., specific antibodies) derived from animal products such as milk may offer the potential for developing specialized food products with prophylactic as well as nutritive quality. This paper discusses the physicochemical mechanism of action of specific bioactive substances naturally present in or derived from foods. The biotechnologies employed to develop these products and the issues concerning acceptance by consumer and regulatory bodies are also addressed.Key words: bioactive substances, food, biotechnology, nutrition.
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Dang, Tam, and Roderich D. Süssmuth. "Bioactive Peptide Natural Products as Lead Structures for Medicinal Use." Accounts of Chemical Research 50, no. 7 (June 26, 2017): 1566–76. http://dx.doi.org/10.1021/acs.accounts.7b00159.
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Gao, Shuman, Yang Jiang, Xinyi Zhang, Shumao Cui, Xiaoming Liu, Jianxin Zhao, Hao Zhang, and Wei Chen. "Comparative Peptidomics Analysis of Milk Fermented by Lactobacillus helveticus." Foods 11, no. 23 (December 1, 2022): 3885. http://dx.doi.org/10.3390/foods11233885.
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Lactobacillus helveticus is one of the commonly used starter cultures for manufacturing various fermented dairy products. However, only a few studies have explored the cleavage region preference of L. helveticus with different cell envelope proteinase (CEP) genes. In the present study, we profiled the peptide composition of milk samples fermented by three different L. helveticus strains by means of peptidomics to illustrate their different proteolysis patterns. The result revealed that the differences in peptide profiles of milk samples fermented by different L. helveticus strains were mainly a result of variations in the peptide patterns of the casein fractions, which were correlated with CEP genotypes. This was mainly reflected in the extensiveness of the hydrolysis region of αS1-casein and the degree of β-casein hydrolysis. Bioactive peptides were mostly derived from the hydrolysis region common to the three L. helveticus strains, and DQHXN-Q32M42 fermentation resulted in the highest diversity and abundance of bioactive peptides and a significant antihypertensive effect in spontaneous hypertension rats.
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Milenteva, Irina, Natalia Davydenko, and Aleksandr Rasshchepkin. "Casein Proteolysis in Bioactive Peptide Production: Optimal Operating Parameters." Food Processing: Techniques and Technology 50, no. 4 (December 30, 2020): 726–35. http://dx.doi.org/10.21603/2074-9414-2020-4-726-735.
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Introduction. Public health is gradually deteriorating as a result of unhealthy lifestyle and diet, which triggers allergic reaction to certain foods. Milk and dairy products are rich in biologically active substances, which makes them a good dietary supplement for athletes, diabetic patients, etc. However, this popular food contains allergens, for instance, such proteins as αS1-casein, αS2-casein, β-casein, and κ-casein. Therefore, one of the most urgent tasks of modern food science is to reduce the allergenic properties of casein. Heat treatment is an option, but thermal exposure leads to denaturation and produces new antigenic determinants, e.g. epitopes.
Biotechnological processing is a more promising method. It is based on the catalytic properties of proteolytic enzymes. Enzymes make it possible to obtain a protein hydrolyzate with amino acids of various molecular weights. The present research provided the optimal working parameters of casein proteolysis by various enzymes (endopectidases), namely trypsin, chymotrypsin, and thermolysin.
Study objects and methods. Casein hydrolysates are casein-based biopeptides, and casein is an accessible and valuable milk protein. Trypsin, chymotrypsin, and thermolysin were used as proteases. The experiment was based on standard methods. Results and its discussion. At 47 ± 2°C and pH 7.5 ± 0.2, the production of low-molecular-weight components of casein hydrolyzate proved feasible when thermolysin was used at a ratio of 1:100 for 24.00 ± 0.05 h, and chymotrypsin and trypsin – at a ratio of 1:25 for 24.00 ± 0.05 h.
Conclusion. The resulting casein hydrolysates contain biologically active peptides and can be used in formulations of low-allergy functional dairy products in allergy-friendly, sports, and baby diets.
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Zhou, Leyi, Rufa L. Mendez, and Jung Yeon Kwon. "In Silico Prospecting for Novel Bioactive Peptides from Seafoods: A Case Study on Pacific Oyster (Crassostrea gigas)." Molecules 28, no. 2 (January 9, 2023): 651. http://dx.doi.org/10.3390/molecules28020651.
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Pacific oyster (Crassostrea gigas), an abundant bivalve consumed across the Pacific, is known to possess a wide range of bioactivities. While there has been some work on its bioactive hydrolysates, the discovery of bioactive peptides (BAPs) remains limited due to the resource-intensive nature of the existing discovery pipeline. To overcome this constraint, in silico-based prospecting is employed to accelerate BAP discovery. Major oyster proteins were digested virtually under a simulated gastrointestinal condition to generate virtual peptide products that were screened against existing databases for peptide bioactivities, toxicity, bitterness, stability in the intestine and in the blood, and novelty. Five peptide candidates were shortlisted showing antidiabetic, anti-inflammatory, antihypertensive, antimicrobial, and anticancer potential. By employing this approach, oyster BAPs were identified at a faster rate, with a wider applicability reach. With the growing market for peptide-based nutraceuticals, this provides an efficient workflow for candidate scouting and end-use investigation for targeted functional product preparation.
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Ghalamara, Soudabeh, Sara Silva, Carla Brazinha, and Manuela Pintado. "Valorization of Fish by-Products: Purification of Bioactive Peptides from Codfish Blood and Sardine Cooking Wastewaters by Membrane Processing." Membranes 10, no. 3 (March 13, 2020): 44. http://dx.doi.org/10.3390/membranes10030044.
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Codfish blood and sardine cooking wastewaters were processed using membrane ultrafiltration that allowed for the preparation of bioactive peptides enriched fractions. The raw materials and corresponding permeates were characterized chemically and in terms of biological properties. The fractionation process was evaluated by analyzing the selective permeation of small peptides (<1 kDa) from larger compounds when using membranes with different molecular weight cut-offs (MWCOs) combined with different materials (MW, PW, and UP010 for codfish blood) and when operated at different transmembrane pressures (with GH for sardine cooking wastewaters). A rejection of the protein/peptides >10 kDa was achieved for both raw materials with the studied membranes. Also, low values of rejection of peptides <1 kDa were accomplished, namely 2% with UP010 from codfish blood and 23% when operated at minimum pressure (1.0 bar) with GH from sardine wastewaters. The peptide fractions from codfish blood with MW and UP010 exhibited the highest ABTS+ and ORAC values. Peptide fractions from sardine wastewaters with GH demonstrated no improvement in antioxidant activity compared to sardine wastewaters. The antimicrobial results showed that the peptide fractions from codfish blood with UP010 and from sardine with GH at 1.0 bar were capable of inhibiting Escherichia coli growth.
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Khvostov, D. V., N. L. Vostrikova, and I. M. Chernukha. "Methodology for the identification of bioactive and marker peptides in the organs of cattle and pigs." Theory and practice of meat processing 7, no. 2 (July 24, 2022): 118–24. http://dx.doi.org/10.21323/2414-438x-2022-7-2-118-124.
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The development of general conception methodology for the meat-based functional food compositions is especially relevant today due to the growing consumers’ interest and attention to their health. This category of these food-products is intended for personal ized nutrition of various age groups in the population, taking into account fortification of the food with nutraceuticals and with functional and metabolically active ingredients obtained from animal and vegetable source. Therefore, it was necessary to develop a certain tool for reliable identification of free peptides from the offals (by-products like hearts and aorta from Sus scrofa and Bos taurus) and from the ready-to-consume meat food (canned food) based on the free peptides, which food is potentially targeted to help with some issues in the human body. The authors proposed the methodology for identification of peptides weighing less than 5 kDa. This methodology has a row of significant advantages, such as a short time of analysis (90 minutes) and the possibility to prepare a large number of samples simultaneously (n=16). Analysis of bioactive peptides (BAPs) was performed by liquid chro matography combined with time-of-flight mass spectrometry (Agilent 6545XT AdvanceBio LC/Q-TOF). The marker peptides were detected by a triple quadrupole mass spectrometer (Agilent 6410 Triple Quadrupole LC/MS). All peptide sequences were defined with the help of mass spectrometric data processing databases like PepBank, BioPep, AHTPDB. In this work from 39 to 269 peculiar soluble peptides were found, with an extraction level of 0.17–0.23%. The main fraction consisted of short peptides less than 1000 Da (71.0–98.0%). In experimental samples of pork hearts and arteries 7 peculiar marker peptides were identified. FFESFGDL SNADAVMGNPK peptide obtained from the β-hemoglobin protein is of a special interest, as this peptide showed the maximum intensity of a signal. Presumably, this peptide can serve as an indicator of the blood presence in the finished food product. So it can serve as an assessment tool of bleeding degree of meat raw. For pork aortas a specific peptide TVLGNFAAFVQK was isolated from serum albumin, which turned out to be stable during heat treatment. This is also important for assessment of meat food that are subjected to high thermal exposure.
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Paulus, Constanze, Josef Zapp, and Andriy Luzhetskyy. "New Scabimycins A-C Isolated from Streptomyces acidiscabies (Lu19992)." Molecules 26, no. 19 (September 29, 2021): 5922. http://dx.doi.org/10.3390/molecules26195922.
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Peptide natural products displaying a wide range of biological activities have become important drug candidates over the years. Microorganisms have been a powerful source of such bioactive peptides, and Streptomyces have yielded many novel natural products thus far. In an effort to uncover such new, meaningful compounds, the metabolome of Streptomyces acidiscabies was analyzed thoroughly. Three new compounds, scabimycins A–C (1–3), were discovered, and their chemical structures were elucidated by NMR spectroscopy. The relative and absolute configurations were determined using ROESY NMR experiments and advanced Marfey’s method.
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Kononiuk, Anna D., and Małgorzata Karwowska. "Bioactive Compounds in Fermented Sausages Prepared from Beef and Fallow Deer Meat with Acid Whey Addition." Molecules 25, no. 10 (May 22, 2020): 2429. http://dx.doi.org/10.3390/molecules25102429.
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The present study examined the effect of the type of meat (beef and fallow deer) and the addition of freeze-dried acid whey on nutritional values and the content of bioactive compounds (peptides, L-carnitine, glutathione, and conjugated linoleic acid (CLA)) in uncured fermented sausages. The antioxidant properties of isolated peptides (ABTS, DPPH radical scavenging activity, and ferric-reducing antioxidant power) were also evaluated. The results showed that fallow deer sausages had higher peptide content than beef products. The addition of acid whey caused a decrease in the content of peptides, especially in fallow deer sausages. The glutathione content in beef sausages (22.91–25.28 mg 100 g−1 of sausage) was quite higher than that of fallow deer sausages (10.04–11.59 mg 100 g−1 of sausage). The obtained results showed a significantly higher content of CLA in beef sausages than in products from fallow deer meat. In conclusion, products prepared from fallow deer meat have generally higher nutritional value because of the content of peptides, their antioxidant properties, and the content of L-carnitine, while beef products have higher levels of CLA and glutathione.
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Mazloomi, Seyadeh Narges, Leticia Mora, M.-Concepción Aristoy, Alireza Sadeghi Mahoonak, Mohammad Ghorbani, Gholamreza Houshmand, and Fidel Toldrá. "Impact of Simulated Gastrointestinal Digestion on the Biological Activity of an Alcalase Hydrolysate of Orange Seed (Siavaraze, Citrus sinensis) by-Products." Foods 9, no. 9 (September 2, 2020): 1217. http://dx.doi.org/10.3390/foods9091217.
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In this study, orange seed proteins were hydrolyzed by Alcalase enzyme at different enzyme concentrations 1–3% (v/w) and hydrolysis times (2–5 h), to obtain bioactive peptides showing antioxidant, Angiotensin-converting enzyme (ACE) -inhibitory, and hypoglycemic activities. The highest biological activities (p < 0.05) were achieved by using a hydrolysis time of 5 h and an enzyme concentration of 2%. Orange seed protein hydrolysate (OSPH) was prepared under these conditions, and peptides were isolated and purified by using size-exclusion chromatography and high-performance liquid chromatography, respectively. The fractions that showed the highest biological activities were analyzed by mass spectrometry in tandem, and a total of 63 peptide sequences were found. Moreover, the effect of simulated gastrointestinal digestion on the bioactivity of the fractions was studied, and the novel peptide sequences generated were also identified. Overall, despite there being some differences in the profile of peptide sequences obtained, the main results showed non-significant differences in the analyzed bioactivities after simulated gastrointestinal digestion.
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Pirrung, Michael C., Fa Zhang, Sudhakar Ambadi, and Y. Gangadhara Rao. "Total synthesis of fellutamides, lipopeptide proteasome inhibitors. More sustainable peptide bond formation." Organic & Biomolecular Chemistry 14, no. 35 (2016): 8367–75. http://dx.doi.org/10.1039/c6ob01233g.
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Basilicata, Manuela Giovanna, Giacomo Pepe, Shara Francesca Rapa, Fabrizio Merciai, Carmine Ostacolo, Michele Manfra, Veronica Di Sarno, et al. "Anti-Inflammatory and Antioxidant Properties of Dehydrated Potato-Derived Bioactive Compounds in Intestinal Cells." International Journal of Molecular Sciences 20, no. 23 (December 3, 2019): 6087. http://dx.doi.org/10.3390/ijms20236087.
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Inflammation and oxidative stress are always more recognized as responsible for chronic disease at the intestinal level. Currently, a growing interest is addressed to the discovery of diet-derived products which have anti-inflammatory and antioxidant properties. This work aims to characterize the pharmacological potential of dehydrated potatoes. For this purpose, a simulated gastrointestinal digestion was carried out. The bioaccessible peptides were fractionated on the basis of their molecular weight and tested on intestinal epithelial cells (IEC-6) under oxidative and inflammatory conditions. Our results demonstrate that the tested peptide fractions were able to significantly inhibit tumor necrosis factor-α release and cycloxygenase-2 and inducible nitric oxide synthase expression. The tested peptides also showed significant antioxidant activity, being able to both reduce reactive oxygen species (ROS) release, also from mitochondria, and nitrotyrosine formation, and increase the antioxidant response by heme oxygenase-1 and superoxide dismutase expression. Moreover, the peptide fractions were able to significantly increase the wound repair in IEC-6. The obtained results indicate the anti-inflammatory and antioxidant potential of dehydrated potatoes at the intestinal level.
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Messina, Concetta Maria, Simona Manuguerra, Rosaria Arena, Giuseppe Renda, Giovanna Ficano, Mariano Randazzo, Stefano Fricano, Saloua Sadok, and Andrea Santulli. "In Vitro Bioactivity of Astaxanthin and Peptides from Hydrolisates of Shrimp (Parapenaeus longirostris) By-Products: From the Extraction Process to Biological Effect Evaluation, as Pilot Actions for the Strategy “From Waste to Profit”." Marine Drugs 19, no. 4 (April 13, 2021): 216. http://dx.doi.org/10.3390/md19040216.
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Non-edible parts of crustaceans could be a rich source of valuable bioactive compounds such as the carotenoid astaxanthin and peptides, which have well-recognized beneficial effects. These compounds are widely used in nutraceuticals and pharmaceuticals, and their market is rapidly growing, suggesting the need to find alternative sources. The aim of this work was to set up a pilot-scale protocol for the reutilization of by-products of processed shrimp, in order to address the utilization of this valuable biomass for nutraceutical and pharmaceuticals application, through the extraction of astaxanthin-enriched oil and antioxidant-rich protein hydrolysates. Astaxanthin (AST) was obtained using “green extraction methods,” such as using fish oil and different fatty acid ethyl esters as solvents and through supercritical fluid extraction (SFE), whereas bioactive peptides were obtained by protease hydrolysis. Both astaxanthin and bioactive peptides exhibited bioactive properties in vitro in cellular model systems, such as antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities (IA). The results show higher astaxanthin yields in ethyl esters fatty acids (TFA) extraction and significant enrichment by short-path distillation (SPD) up to 114.80 ± 1.23 µg/mL. Peptide fractions of <3 kDa and 3–5 kDa exhibited greater antioxidant activity while the fraction 5–10 kDa exhibited a better ACE-IA. Lower-molecular-weight bioactive peptides and astaxanthin extracted using supercritical fluids showed protective effects against oxidative damage in 142BR and in 3T3 cell lines. These results suggest that “green” extraction methods allow us to obtain high-quality bioactive compounds from large volumes of shrimp waste for nutraceutical and pharmaceutical applications.
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Donadio, Giuliana, Valentina Santoro, Fabrizio Dal Piaz, and Nunziatina De Tommasi. "Food Matrices Affect the Peptides Produced during the Digestion of Arthrospira platensis-Based Functional Aliments." Nutrients 13, no. 11 (November 1, 2021): 3919. http://dx.doi.org/10.3390/nu13113919.
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Arthrospira platensis (Spirulina) has been credited with multiple beneficial effects, many of which are attributed to bioactive peptides produced during the gastrointestinal digestion of this micro-alga. Many Spirulina-based nutraceuticals have been produced, and numerous functional foods enriched with Spirulina are available on the market. These are subjected to checks aimed at verifying the amount of algae actually present, but few studies relating to the bioavailability of the bioactive compounds in these products have been carried out. However, such investigations could be very important to elucidate the possible critical effects exerted by food matrices on protein digestion and bioactive peptide production. Here, in order to assess the suitability of Spirulina-enriched foods as a source of potentially bioactive peptides, a simulated digestion protocol was used in combination with mass spectrometry quantitative analysis to analyze functionalized pasta and sorbets. In the case of the pasta enriched with Spirulina, the production of peptides was quite similar to that of the Spirulina powder. On the other hand, the type of fruit present in the food matrix influenced the digestion of Spirulina inside the sorbets. In particular, the high concentration of protease inhibitors in kiwifruit drastically reduced the production of peptides from Spirulina in kiwi sorbet.
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Sabir Mustafayeva, Rugiya. "EFFECT OF STRAIN ENTEROCOCCUS FAECALIS AN1 ON RELEASE OF BIOACTIVE PEPTIDES FROM WHEY PROTEINS IN IN VITRO SIMULATED GASTROINTESTINAL CONDITIONS." NATURE AND SCIENCE 03, no. 04 (October 27, 2020): 64–68. http://dx.doi.org/10.36719/2707-1146/04/64-68.
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The aim of the study was to study the potential of the proteolytic strain Enterococcus faecalis AN1 to generate inhibition of angiotensin converting enzyme (ACE), as well as to determine the effect of subsequent hydrolysis with pepsin and pancreatin in vitro simulated gastrointestinal system on this activity. Analysis of substrate hydrolysis and peptide formation was performed using SDS-PAGE and electrophoresis by RP-HPLC. Casein hydrolyzate with proteases of the strain showed the ability to produce peptides with ACE inhibition activity, which shows the use of these strains in the development of functional dairy products with antihypertensive properties. The studied strain has the potential to produce functional dairy products. Key words: lactic acid bacteria, proteases, caseins, bioactive peptides, angiotensin converting enzyme
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Montone, Carmela Maria, Sara Elsa Aita, Chiara Cavaliere, Andrea Cerrato, Aldo Laganà, Susy Piovesana, and Anna Laura Capriotti. "High-Resolution Mass Spectrometry and Chemometrics for the Detailed Characterization of Short Endogenous Peptides in Milk By-Products." Molecules 26, no. 21 (October 27, 2021): 6472. http://dx.doi.org/10.3390/molecules26216472.
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The process of cheese-making has long been part of human food culture and nowadays dairy represents a large sector of the food industry. Being the main byproduct of cheese-making, the revalorization of milk whey is nowadays one of the primary goals in alignment with the principles of the circular economy. In the present paper, a deep and detailed investigation of short endogenous peptides in milk and its byproducts (whole whey, skimmed whey, and whey permeate) was carried out by high-resolution mass spectrometry, with a dedicated suspect screening data acquisition and data analysis approach. A total of 79 short peptides was tentatively identified, including several sequences already known for their exerted biological activities. An unsupervised chemometric approach was then employed for highlighting the differences in the short peptide content among the four sets of samples. Whole and skimmed whey showed not merely a higher content of short bioactive peptides compared to whole milk, but also a peculiar composition of peptides that are likely generated during the process of cheese-making. The results clearly demonstrate that whey represents a valuable source of bioactive compounds and that the set-up of processes of revalorization of milk byproducts is a promising path in the obtention of high revenue-generating products from dairy industrial waste.
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Zhou, Xiao Li, Xiao Xiao Meng, Qing Wang, Yi Ming Zhou, and Zong Jie Li. "Comparative Anti-Tumor Activity Study of Tartary Buckwheat Flavonoids and Amphibian Peptides." Advanced Materials Research 781-784 (September 2013): 1270–74. http://dx.doi.org/10.4028/www.scientific.net/amr.781-784.1270.
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In China, many kinds of natural products extracted from plant and animal were used to treat cancer. Flavonoids extracted from tartary buckwheat and skin peptide purified from rufous-spotted torrent frog had respectively been proved to have anti-tumor activity. In present study, both tartary buckwheat flavonoids and amphibian frog peptides were applied for cell proliferation inhibitory activity against human gastric cancer MGC 80-3 cells using MTT assay. According to the data, the buckwheat flavonoids exhibited much stronger anti-tumor activity than amphibian peptides, and the complex mixture of this two kinds of bioactive compounds still possess anti-tumor activity.
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Martini, Serena, Lisa Solieri, Alice Cattivelli, Valentina Pizzamiglio, and Davide Tagliazucchi. "An Integrated Peptidomics and In Silico Approach to Identify Novel Anti-Diabetic Peptides in Parmigiano-Reggiano Cheese." Biology 10, no. 6 (June 21, 2021): 563. http://dx.doi.org/10.3390/biology10060563.
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Inhibition of key metabolic enzymes linked to type-2-diabetes (T2D) by food-derived compounds is a preventive emerging strategy in the management of T2D. Here, the impact of Parmigiano-Reggiano (PR) cheese peptide fractions, at four different ripening times (12, 18, 24, and 30 months), on the enzymatic activity of α-glucosidase, α-amylase, and dipeptidyl peptidase-IV (DPP-IV) as well as on the formation of fluorescent advanced glycation end-products (fAGEs) was assessed. The PR peptide fractions were able to inhibit the selected enzymes and fAGEs formation. The 12-month-ripening PR sample was the most active against the three enzymes and fAGEs. Mass spectrometry analysis enabled the identification of 415 unique peptides, 54.9% of them common to the four PR samples. Forty-nine previously identified bioactive peptides were found, mostly characterized as angiotensin-converting enzyme-inhibitors. The application of an integrated approach that combined peptidomics, in silico analysis, and a structure–activity relationship led to an efficient selection of 6 peptides with potential DPP-IV and α-glucosidase inhibitory activities. Peptide APFPE was identified as a potent novel DPP-IV inhibitor (IC50 = 49.5 ± 0.5 μmol/L). In addition, the well-known anti-hypertensive tripeptide, IPP, was the only one able to inhibit the three digestive enzymes, highlighting its possible new and pivotal role in diabetes management.
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Vetrichelvan, Muthalagu, Vijayabhaskar Bokkala, Surendran Renganathan, Arvind Mathur, Richard Rampulla, and Anuradha Gupta. "A Short and Scalable Synthesis of Orthogonally Protected Bis(aminomethyl)malonic Acid: Access to Bioactive Macrocyclic Peptides." Synthesis 49, no. 22 (August 1, 2017): 5039–44. http://dx.doi.org/10.1055/s-0036-1588505.
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A short and scalable process for the preparation of multi-gram quantities of orthogonally protected bis(aminomethyl)malonic acid in good yield from readily available starting material is described. These orthogonally protected amino acids are important building blocks to make peptides based drugs, glycoconjugates, and in the total synthesis of peptide natural products. The newly developed route has only six steps with an overall yield of 27%, which involves nucleophilic attack of a malonate on an imide as one of the key steps.
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Hebert, Elvira María, Gianfranco Mamone, Gianluca Picariello, Raúl R. Raya, Graciela Savoy, Pasquale Ferranti, and Francesco Addeo. "Characterization of the Pattern of αs1- and β-Casein Breakdown and Release of a Bioactive Peptide by a Cell Envelope Proteinase from Lactobacillus delbrueckii subsp. lactis CRL 581." Applied and Environmental Microbiology 74, no. 12 (April 18, 2008): 3682–89. http://dx.doi.org/10.1128/aem.00247-08.
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ABSTRACT The cell envelope-associated proteinases (CEPs) of the lactobacilli have key roles in bacterial nutrition and contribute to the development of the organoleptic properties of fermented milk products as well, as they can release bioactive health-beneficial peptides from milk proteins. The influence of the peptide supply, carbohydrate source, and osmolites on the CEP activity of the cheese starter Lactobacillus delbrueckii subsp. lactis CRL 581 was investigated. The CEP activity levels were controlled by the peptide content of the growth medium. The maximum activity was observed in a basal minimal defined medium, whereas in the presence of Casitone, Casamino Acids, or yeast extract, the synthesis of CEP was inhibited 99-, 70-, and 68-fold, respectively. The addition of specific di- or tripeptides containing branched-chain amino acids, such as leucylleucine, prolylleucine, leucylglycylglycine, or leucylproline, to the growth medium negatively affected CEP activity, whereas dipeptides without branched-chain amino acids had no effect on the enzyme's production. The carbon source and osmolites did not affect CEP activity. The CEP of L. delbrueckii subsp. lactis CRL 581 exhibited a mixed-type CEPI/III variant caseinolytic specificity. Mass-spectrometric screening of the main peptide peaks isolated by reverse-phase high-pressure liquid chromatography allowed the identification of 33 and 32 peptides in the αs1- and β-casein hydrolysates, respectively. By characterizing the peptide sequence in these hydrolysates, a pattern of αs1- and β-casein breakdown was defined and is reported herein, this being the first report for a CEP of L. delbrueckii subsp. lactis. In this pattern, a series of potentially bioactive peptides (antihypertensive and phosphopeptides) which are encrypted within the precursor protein could be visualized.
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Senokosova, E. A., E. O. Krivkina, L. V. Antonova, and L. S. Barbarash. "Biodegradable small-diameter vascular graft: types of modification with bioactive molecules and RGD peptides." Russian Journal of Transplantology and Artificial Organs 22, no. 1 (April 23, 2020): 86–96. http://dx.doi.org/10.15825/1995-1191-2020-1-86-96.
Full textAbstract:
The need for small-diameter grafts for replacing the damaged area of the blood pool is still very high. These grafts are very popular for coronary artery bypass grafting. Polymeric synthetic grafts are an alternative to autografts. A promising area of tissue engineering is the creation of a biodegradable graft. It can serve as the basis for de novo generation of vascular tissue directly in the patient’s body. Optimization of the polymer composition of products has led to improved physicomechanical and biocompatible properties of the products. However, the improvements are still far from needed. One of the decisive factors in the reliability of a small-diameter vascular graft is the early formation of endothelial lining on its inner surface, which can provide atrombogenic effect and full lumen of the future newly formed vessel. To achieve this goal, grafts are modified by incorporating bioactive molecules or functionally active peptide sequences into the polymer composition or immobilizing on its inner surface. Peptide sequences include cell adhesion site – arginine-glycine-aspartic acid (RGD peptide). This sequence is present in most extracellular matrix proteins and has a tropism for integrin receptors of endothelial cells. Many studies have shown that imitation of the functional activity of the natural extracellular matrix can promote spontaneous endothelization of the inner surface of a vascular graft. Moreover, configuration of the RGD peptide determines the survival and differentiation of endothelial cells. The linker through which the peptide is crosslinked to the polymer surface determines the bioavailability of the RGD peptide for endothelial cells.
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Montone, Carmela Maria, Riccardo Zenezini Chiozzi, Nicola Marchetti, Andrea Cerrato, Michela Antonelli, Anna Laura Capriotti, Chiara Cavaliere, Susy Piovesana, and Aldo Laganà. "Peptidomic Approach for the Identification of Peptides with Potential Antioxidant and Anti-Hyperthensive Effects Derived From Asparagus By-Products." Molecules 24, no. 19 (October 8, 2019): 3627. http://dx.doi.org/10.3390/molecules24193627.
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Asparagus waste represents products of great interest since many compounds with high biological value are located in the lower portion of the spears. The extraction of bioactive compounds from asparagus by-products is therefore crucial for the purpose of adding value to these by-products. In this paper, bioactive peptides from asparagus waste were extracted, digested, purified and identified. In particular, Alcalase® was chosen as the enzyme to use to obtain protein hydrolysate due to its low cost and, consequently, the possibility of implementing the method on a large scale. In order to simplify the peptide extract to reach better identification, the hydrolysate was fractionated by reversed-phase chromatography in 10 fractions. Two tests were carried out for antioxidant activity (ABTS-DPPH) and one for antihypertensive activity (ACE). Fractions with a higher bioactivity score were identified by peptidomics technologies and screened for bioactivity with the use of bioinformatics. For ACE-inhibitor activity, two peptides were synthetized, PDWFLLL and ASQSIWLPGWL, which provided an EC50 value of 1.76 µmol L−1 and 4.02 µmol L−1, respectively. For the antioxidant activity, by DPPH assay, MLLFPM exhibited the lowest EC50 value at 4.14 µmol L−1, followed by FIARNFLLGW and FAPVPFDF with EC50 values of 6.76 µmol L−1 and 10.01 µmol L−1, respectively. A validation of the five identified peptides was also carried out. The obtained results showed that peptides obtained from asparagus by-products are of interest for their biological activity and are suitable for being used as functional ingredients.
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Chaipoot, Supakit, Wanisa Punfa, Sakaewan Ounjaijean, Rewat Phongphisutthinant, Kanokwan Kulprachakarn, Wason Parklak, Laddawan Phaworn, Pattrawan Rotphet, and Kongsak Boonyapranai. "Antioxidant, Anti-Diabetic, Anti-Obesity, and Antihypertensive Properties of Protein Hydrolysate and Peptide Fractions from Black Sesame Cake." Molecules 28, no. 1 (December 26, 2022): 211. http://dx.doi.org/10.3390/molecules28010211.
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A low-value by-product of cold-pressed sesame oil is defatted black sesame cake (DBSC). The remaining protein and essential amino acids may be utilized as a renewable biological source to produce bioactive products. The bioactivities of the protein hydrolysate from black sesame cake and its peptide fractions were examined in this study for in vitro antioxidant activity and inhibition of DPP-IV, ACE, α-amylase, α-glucosidase, and pancreatic lipase. By using Flavourzyme to hydrolyze DBSC, followed by ultrafiltration, fractions with peptide sizes of <3, 3–10, and >10 kDa were obtained. According to the findings, the products of DBSC could neutralize free radicals and prevent ferric ion redox reactions. The highest inhibitory effects were shown with low Mw peptides (<3 kDa) against ACE, DPP-IV, α-amylase, and α-glucosidase. DBSC has demonstrated potential as a nutraceutical or functional ingredient for preventing and treating disorders associated with free radicals, such as diabetes, hypertension, and hyperglycemia.
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Tomazou, Marios, Anastasis Oulas, Athanasios K. Anagnostopoulos, George Th Tsangaris, and George M. Spyrou. "In Silico Identification of Antimicrobial Peptides in the Proteomes of Goat and Sheep Milk and Feta Cheese." Proteomes 7, no. 4 (September 21, 2019): 32. http://dx.doi.org/10.3390/proteomes7040032.
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Milk and dairy products are a major functional food group of growing scientific and commercial interest due to their nutritional value and bioactive “load”. A major fraction of the latter is attributed to milk’s rich protein content and its biofunctional peptides that occur naturally during digestion. On the basis of the identified proteome datasets of milk whey from sheep and goat breeds in Greece and feta cheese obtained during previous work, we applied an in silico workflow to predict and characterise the antimicrobial peptide content of these proteomes. We utilised existing tools for predicting peptide sequences with antimicrobial traits complemented by in silico protein cleavage modelling to identify frequently occurring antimicrobial peptides (AMPs) in the gastrointestinal (GI) tract in humans. The peptides of interest were finally assessed for their stability with respect to their susceptibility to cleavage by endogenous proteases expressed along the intestinal part of the GI tract and ranked with respect to both their antimicrobial and stability scores.
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Ries, Oliver, Martin Büschleb, Markus Granitzka, Dietmar Stalke, and Christian Ducho. "Amino acid motifs in natural products: synthesis of O-acylated derivatives of (2S,3S)-3-hydroxyleucine." Beilstein Journal of Organic Chemistry 10 (May 16, 2014): 1135–42. http://dx.doi.org/10.3762/bjoc.10.113.
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(2S,3S)-3-Hydroxyleucine can be found in an increasing number of bioactive natural products. Within the context of our work regarding the total synthesis of muraymycin nucleoside antibiotics, we have developed a synthetic approach towards (2S,3S)-3-hydroxyleucine building blocks. Application of different protecting group patterns led to building blocks suitable for C- or N-terminal derivatization as well as for solid-phase peptide synthesis. With respect to according motifs occurring in natural products, we have converted these building blocks into 3-O-acylated structures. Utilizing an esterification and cross-metathesis protocol, (2S,3S)-3-hydroxyleucine derivatives were synthesized, thus opening up an excellent approach for the synthesis of bioactive natural products and derivatives thereof for structure activity relationship (SAR) studies.
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Offret, Clément, Ismaïl Fliss, Laurent Bazinet, André Marette, and Lucie Beaulieu. "Identification of A Novel Antibacterial Peptide from Atlantic Mackerel belonging to the GAPDH-Related Antimicrobial Family and Its In Vitro Digestibility." Marine Drugs 17, no. 7 (July 12, 2019): 413. http://dx.doi.org/10.3390/md17070413.
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The Atlantic mackerel, Scomber scombrus, is one of the most fished species in the world, but it is still largely used for low-value products, such as bait; mainly for crustacean fishery. This resource could be transformed into products of high value and may offer new opportunities for the discovery of bioactive molecules. Mackerel hydrolysate was investigated to discover antibacterial peptides with biotechnological potential. The proteolytic process generated a hydrolysate composed of 96% proteinaceous compounds with molecular weight lower than 7 kDa. From the whole hydrolysate, antibacterial activity was detected against both Gram-negative and Gram-positive bacteria. After solid phase extraction, purification of the active fraction led to the identification of 4 peptide sequences by mass spectrometry. The peptide sequence N-KVEIVAINDPFIDL-C, called Atlantic Mackerel GAPDH-related peptide (AMGAP), was selected for chemical synthesis to confirm the antibacterial activity and to evaluate its stability through in vitro digestibility. Minimal inhibitory concentrations of AMGAP revealed that Listeria strains were the most sensitive, suggesting potential as food-preservative to prevent bacterial growth. In addition, in vitro digestibility experiments found rapid (after 20 min) and early digestibility (stomach). This study highlights the biotechnological potential of mackerel hydrolysate due to the presence of the antibacterial AMGAP peptide.
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Lacey, Heather J., and Peter J. Rutledge. "Recently Discovered Secondary Metabolites from Streptomyces Species." Molecules 27, no. 3 (January 28, 2022): 887. http://dx.doi.org/10.3390/molecules27030887.
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The Streptomyces genus has been a rich source of bioactive natural products, medicinal chemicals, and novel drug leads for three-quarters of a century. Yet studies suggest that the genus is capable of making some 150,000 more bioactive compounds than all Streptomyces secondary metabolites reported to date. Researchers around the world continue to explore this enormous potential using a range of strategies including modification of culture conditions, bioinformatics and genome mining, heterologous expression, and other approaches to cryptic biosynthetic gene cluster activation. Our survey of the recent literature, with a particular focus on the year 2020, brings together more than 70 novel secondary metabolites from Streptomyces species, which are discussed in this review. This diverse array includes cyclic and linear peptides, peptide derivatives, polyketides, terpenoids, polyaromatics, macrocycles, and furans, the isolation, chemical structures, and bioactivity of which are appraised. The discovery of these many different compounds demonstrates the continued potential of Streptomyces as a source of new and interesting natural products and contributes further important pieces to the mostly unfinished puzzle of Earth’s myriad microbes and their multifaceted chemical output.
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Pugliese, Raffaele, Martina Bartolomei, Carlotta Bollati, Giovanna Boschin, Anna Arnoldi, and Carmen Lammi. "Gel-Forming of Self-Assembling Peptides Functionalized with Food Bioactive Motifs Modulate DPP-IV and ACE Inhibitory Activity in Human Intestinal Caco-2 Cells." Biomedicines 10, no. 2 (January 31, 2022): 330. http://dx.doi.org/10.3390/biomedicines10020330.
Full textAbstract:
Food bioactive peptides are increasingly used for formulating food products, nutraceuticals, and functional food, since they are generally considered safe for human consumption and metabolic syndrome prevention. They are also becoming popular as sustainable sources of novel functional biomaterials such as hydrogels, edible nanonutraceuticals, delivery systems, and packing materials. However, such food peptides are mostly unstable, and degrade during food processing, or in a gastrointestinal environment, thus resulting in low bioavailability precluding their practical applications. Here, we decided to functionalize the well-known and characterized self-assembling peptide RADA16 with two synthetic analogues of food bioactive peptides deriving from the hydrolysis of soybean glycinin and lupin β-conglutin (namely IAVPTGVA and LTFPGSAED) for control of and improvement in their gel-forming nanostructures, biomechanics, and biological features. Extensive characterization was performed via Circular Dichroism (CD) spectroscopy, Fourier Transform Infrared spectroscopy (FT-IR), Thioflavin T (ThT) binding assay, rheological measurements, and Atomic Force Microscopy (AFM) analysis. Lastly, since self-assembling peptides (SAPs) can be co-assembled with diluent SAPs (without a bioactive epitope) as an approach to control the density of biological signals and therefore attain enhanced bioactivity, we investigated the effect of the co-assembly of RADA16 and functionalized food bioactive SAPs (dubbed cAP-Soy1 and cAP-Lup1) for the growth of Caco-2 human intestinal cells and contextually we characterized their biological activities as DPP-IV and ACE inhibitors, in order to demonstrate their potential use for the prevention of metabolic syndrome.
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Mazloomi, Seyadeh Narges, Alireza Sadeghi Mahoonak, Leticia Mora, Mohammad Ghorbani, Gholamreza Houshmand, and Fidel Toldrá. "Pepsin Hydrolysis of Orange By-Products for the Production of Bioactive Peptides with Gastrointestinal Resistant Properties." Foods 10, no. 3 (March 23, 2021): 679. http://dx.doi.org/10.3390/foods10030679.
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Recently, the use of bioactive compounds in improving human health has received more attention. The aim of the present study was to hydrolyze orange seed proteins using pepsin enzyme to obtain bioactive peptides as well as to study the stability of such activity after simulated gastrointestinal digestion conditions. The method was optimized using different enzyme concentrations from 1% to 3%, hydrolysis times between 2 and 5 h, and an optimal temperature of 33 °C. Biological activities including α-glucosidase inhibition, α-amylase inhibition, Angiotensin I-Converting Enzyme (ACEI) inhibition, ferric reducing antioxidant power, and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity were evaluated. According to the results, a significant higher value of the biological activity (p < 0.05) was observed using an enzyme ratio of 0.03 E/S and hydrolysis time of 3.5 h. After size-exclusion chromatography separation, fractions 45–49 and 50–54 showed the highest biological roles such as antioxidant, ACEI inhibitory, and hypoglycemic. Fractions with the highest biological activity were purified using RP-HPLC and analyzed using nano-liquid chromatography and mass spectrometry. The results obtained after simulated gastrointestinal digestion indicated that peptide fractions obtained after chromatographic separation significantly maintain their activity.
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Mendez, Rufa, and Jung Yeon Kwon. "Streamlining Bioactive Peptide Discovery With In Silico Prospecting: An investigation on Seaweed Pacific Dulse." Current Developments in Nutrition 6, Supplement_1 (June 2022): 315. http://dx.doi.org/10.1093/cdn/nzac053.056.
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Abstract Objectives Bioactive hydrolysates and peptides from seaweed sources have been shown to exert beneficial effects in both in vitro and in vivo models for metabolic health. However, the discovery approach relies heavily on the conventional hydrolysate preparation and screening model selection, both driven by resource availability and time constraints. Considering the potential for functional food and therapeutics development, efficient and cost-effective strategies are needed to scope out as much prospect that can be screened for increased chances of hits to find potent, stable, and commercializable bioactive peptides (BAPs). This work aimed to identify multifunctional BAPs from seaweed Pacific Dulse, and to determine which hydrolytic condition can favor the release of more BAPs of interest from this protein-rich macroalgae. Methods Virtual hydrolysates were prepared from dulse proteins using three digestion platforms (ExPASy, SystemsBio, and Rapid Peptide Generator) under three production stream contexts (hydrolysate preparation, gastrointestinal digestion, and microbial fermentation). Peptide products were then subjected to in silico bioactivity prospecting for anti-inflammatory, antidiabetic, and antihypertensive potential. Stability in the intestine and blood was predicted along with potential toxicity. Non-toxic and stable peptides predicted to have multifunctionalities were shortlisted for bioactivity validation, and production streams predicted to generate most number of BAPs were noted for test hydrolysate production. Results With our approach, we identified 13 novel prospect BAPs that have multiple bioactivities, high stability, and low toxicity. Hydrolysate production using bromelain and ficin favored the 5–10aa long mBAPs generation. Simulated gastrointestinal digestion and microbial fermentation also showed promise in the release of some BAPs of interest. Conclusions When consumed in either hydrolyzed, whole, or fermented form, BAPs can be generated from seaweed Pacific Dulse proteins. Bioactivity testing of the novel BAPs identified, and microscale production of the promising BAP production stream are underway. Funding Sources Oregon Agricultural Experiment Station.
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MOHD ZAIN, FATIN ARINA, NORSHAZILA SHAHIDAN, NURUL HUDA, ZARINAH ZAKARIA, and ABDI WIRA SEPTAMA. "ANTIOXIDANT ACTIVITY OF BIOACTIVE PEPTIDE DERIVED FROM PEKIN DUCK FEET GELATIN HYDROLYSATE." Malaysian Applied Biology 49, no. 4 (July 19, 2021): 19–24. http://dx.doi.org/10.55230/mabjournal.v49i4.1563.
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Malaysia is one of the main producers of duck meat globally with increasing demands. Increasing in duck production will also increase the number of duck by-products such as skin, feet and bones. Pekin duck (Anas platyrhyncos domestica) is one of the famous duck breeds. Gelatin that was extracted from Pekin duck feet has shown a potential raw material for the production of bioactive peptide that can involve in various functions of the organism physiologically for example antioxidant effects. Pekin Duck feet gelatin was hydrolyzed by using five commercial enzymes (Alcalase, Esperase, Flavourzyme, Neutrase and Protamex) to identify radical scavenging potencies of derived bioactive peptides. All the five enzymes were studied under three different enzyme-substrate ratio (1:10, 1:15, 1:20) with every enzyme optimum pH and temperature. Scavenging activities studied included DPPH radical scavenging activity and ABTS radical scavenging activity. In DPPH radical scavenging activity, all the five enzymes showed the highest percentage of radical scavenging activity at (1:20) enzyme-substrate ratio condition. Among the five enzymes studied, gelatin hydrolyzed with Protamex showed the highest activity (54.83%), followed by Alcalase (53.12%), Esperase (49.81%), Flavourzyme (49.32%) and lastly Neutrase (47.49%) at sample concentration 4.5 mg/ml. The half-maximal inhibitory concentration (IC50) value of the bioactive peptide for ABTS radical scavenging activity was measured. Alcalase has produced the duck feet gelatin hydrolysate that has the lowest IC50 value against ABTS radical scavenging activity with value (0.45%) followed by Esperase (0.54%), Neutrase (0.57%), Protamex (0.60%) and lastly Flavourzyme (0.74%).
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Henaux, Loïc, Karina Danielle Pereira, Jacinthe Thibodeau, Geneviève Pilon, Tom Gill, André Marette, and Laurent Bazinet. "Glucoregulatory and Anti-Inflammatory Activities of Peptide Fractions Separated by Electrodialysis with Ultrafiltration Membranes from Salmon Protein Hydrolysate and Identification of Four Novel Glucoregulatory Peptides." Membranes 11, no. 7 (July 14, 2021): 528. http://dx.doi.org/10.3390/membranes11070528.
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Natural bioactive peptides are suitable candidates for preventing the development of Type 2 diabetes (T2D), by reducing the various risk factors. The aim of this study was to concentrate glucoregulatory and anti-inflammatory peptides, from salmon by-products, by electrodialysis with ultrafiltration membrane (EDUF), and to identify peptides responsible for these bioactivities. Two EDUF configurations (1 and 2) were used to concentrate anionic and cationic peptides, respectively. After EDUF separation, two fractions demonstrated interesting properties: the initial fraction of the EDUF configuration 1 and the final fraction of the EDUF configuration 2 both showed biological activities to (1) increase glucose uptake in L6 muscle cells in insulin condition at 1 ng/mL (by 12% and 21%, respectively), (2) decrease hepatic glucose production in hepatic cells at 1 ng/mL in basal (17% and 16%, respectively), and insulin (25% and 34%, respectively) conditions, and (3) decrease LPS-induced inflammation in macrophages at 1 g/mL (45% and 30%, respectively). More impressive, the initial fraction of the EDUF configuration 1 (45% reduction) showed the same effect as the phenformin at 10 μM (40%), a drug used to treat T2D. Thirteen peptides were identified, chemically synthesized, and tested in-vitro for these three bioactivities. Thus, four new bioactive peptides were identified: IPVE increased glucose uptake by muscle cells, IVDI and IEGTL decreased hepatic glucose production (HGP) of insulin, whereas VAPEEHPTL decreased HGP under both basal condition and in the presence of insulin. To the best of our knowledge, this is the first time that (1) bioactive peptide fractions generated after separation by EDUF were demonstrated to be bioactive on three different criteria; all involved in the T2D, and (2) potential sequences involved in the improvement of glucose uptake and/or in the regulation of HGP were identified from a salmon protein hydrolysate.
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Kong, Saerom, Hye-Ryung Choi, Yoon-Jeong Kim, Yoon-Sik Lee, Kyoung-Chan Park, and Seon-Yeong Kwak. "Milk Protein-Derived Antioxidant Tetrapeptides as Potential Hypopigmenting Agents." Antioxidants 9, no. 11 (November 10, 2020): 1106. http://dx.doi.org/10.3390/antiox9111106.
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Excessive accumulation of melanin can cause skin pigmentation disorders, which may be accompanied by significant psychological stress. Although many natural and synthetic products have been developed for the regulation of melanogenesis biochemistry, the management of unwanted skin pigmentation remains challenging. Herein, we investigated the potential hypopigmenting properties of peptide sequences that originated from milk proteins such as ĸ-casein and β-lactoglobulin. These proteins are known to inhibit melanogenesis and their hydrolysates are reported as antioxidant peptides. We synthesize tetrapeptide fragments of the milk protein hydrolysates and investigate the amino acids that are essential for designing peptides with tyrosinase inhibitory and antioxidant activities. We found that the peptide methionine-histidine-isoleucine-arginine amide sufficiently inhibits mushroom tyrosinase activity, shows potent antioxidant activity and effectively impedes melanogenesis in cultured melanocytes via cooperative biological activities. Our findings demonstrate the potential utility of the bioactive tetrapeptide from milk proteins as a chemical alternative to hypopigmenting agents.
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Sukmarini, Linda. "Antiviral Peptides (AVPs) of Marine Origin as Propitious Therapeutic Drug Candidates for the Treatment of Human Viruses." Molecules 27, no. 9 (April 19, 2022): 2619. http://dx.doi.org/10.3390/molecules27092619.
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The marine environment presents a favorable avenue for potential therapeutic agents as a reservoir of new bioactive natural products. Due to their numerous potential pharmacological effects, marine-derived natural products—particularly marine peptides—have gained considerable attention. These peptides have shown a broad spectrum of biological functions, such as antimicrobial, antiviral, cytotoxic, immunomodulatory, and analgesic effects. The emergence of new virus strains and viral resistance leads to continuing efforts to develop more effective antiviral drugs. Interestingly, antimicrobial peptides (AMPs) that possess antiviral properties and are alternatively regarded as antiviral peptides (AVPs) demonstrate vast potential as alternative peptide-based drug candidates available for viral infection treatments. Hence, AVPs obtained from various marine organisms have been evaluated. This brief review features recent updates of marine-derived AVPs from 2011 to 2021. Moreover, the biosynthesis of this class of compounds and their possible mechanisms of action are also discussed. Selected peptides from various marine organisms possessing antiviral activities against important human viruses—such as human immunodeficiency viruses, herpes simplex viruses, influenza viruses, hepatitis C virus, and coronaviruses—are highlighted herein.
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Evidente, Antonio. "Bioactive Lipodepsipeptides Produced by Bacteria and Fungi †." International Journal of Molecular Sciences 23, no. 20 (October 15, 2022): 12342. http://dx.doi.org/10.3390/ijms232012342.
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Natural products are a vital source for agriculture, medicine, cosmetics and other fields. Lipodepsipeptides (LPDs) are a wide group of natural products distributed among living organisms such as bacteria, fungi, yeasts, virus, insects, plants and marine organisms. They are a group of compounds consisting of a lipid connected to a peptide, which are able to self-assemble into several different structures. They have shown different biological activities such as phytotoxic, antibiotic, antiviral, antiparasitic, antifungal, antibacterial, immunosuppressive, herbicidal, cytotoxic and hemolytic activities. Their biological activities seem to be due to their interactions with the plasma membrane (MP) because they are able to mimic the architecture of the native membranes interacting with their hydrophobic segment. LPDs also have surfactant properties. The review has been focused on the lipodepsipeptides isolated from fungal and bacterial sources, on their biological activity, on the structure–activity relationships of some selected LPD subgroups and on their potential application in agriculture and medicine. The chemical and biological characterization of lipodepsipeptides isolated in the last three decades and findings that resulted from SCI-FINDER research are reported. A critical evaluation of the most recent reviews dealing with the same argument has also been described.
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Wölk, Michele, Sanja Milkovska-Stamenova, and Ralf Hoffmann. "Comprehensive Profiling of the Native and Modified Peptidomes of Raw Bovine Milk and Processed Milk Products." Foods 9, no. 12 (December 10, 2020): 1841. http://dx.doi.org/10.3390/foods9121841.
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Bovine milk contains a variety of endogenous peptides, partially formed by milk proteases that may exert diverse bioactive functions. Milk storage allows further protease activities altering the milk peptidome, while processing, e.g., heat treatment can trigger diverse chemical reactions, such as Maillard reactions and oxidations, leading to different posttranslational modifications (PTMs). The influence of processing on the native and modified peptidome was studied by analyzing peptides extracted from raw milk (RM), ultra-high temperature (UHT) milk, and powdered infant formula (IF) by nano reversed-phase liquid chromatography coupled online to electrospray ionization (ESI) tandem mass spectrometry. Only unmodified peptides proposed by two independent software tools were considered as identified. Thus, 801 identified peptides mainly originated from αS- and β-caseins, but also from milk fat globular membrane proteins, such as glycosylation-dependent cell adhesion molecule 1. RM and UHT milk showed comparable unmodified peptide profiles, whereas IF differed mainly due to a higher number of β-casein peptides. When 26 non-enzymatic posttranslational modifications (PTMs) were targeted in the milk peptidomes, 175 modified peptides were identified, i.e., mostly lactosylated and a few hexosylated or oxidized peptides. Most modified peptides originated from αS-caseins. The numbers of lactosylated peptides increased with harsher processing.
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Kęska, Paulina, and Joanna Stadnik. "Peptidomic Characteristic of Peptides Generated in Dry-Cured Loins with Probiotic Strains of LAB during 360-Days Aging." Applied Sciences 12, no. 12 (June 14, 2022): 6036. http://dx.doi.org/10.3390/app12126036.
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Peptidomics refers to the comprehensive profiling of endogenous peptides obtained from biological sources. The formation of endogenous peptides is dependent on not only endogenous factors but also exogenous factors such as microbial proteases or process conditions, including fermentation. This study analyzed the probiotic strains of Lactobacillus rhamnosus LOCK900 (LOCK), Bifidobacterium animalis ssp. lactis BB-12 (BB12), and potential probiotic Lactobacillus acidophilus Bauer Ł0938 (BAUER) to assess their ability of fermentation and peptide production in dry-cured pork loin. The peptides obtained after in vitro digestion were characterized by liquid chromatography–tandem mass spectrometry. Based on the sequences identified, the degree of similarity or differences between the peptides was determined and presented graphically on the factor plane. The charts showed that the meat products aged for 180 and 270 days were the most diverse when BB12 or BAUER were used as starter cultures. Myosin and keratin were identified as the most likely precursors of bioactive peptides in products obtained using this strain of lactic acid bacteria (LAB). The knowledge acquired from this study may contribute to the design of functional meat products as the results revealed not only the peptidogenic potential of the LAB strains indicated on their beneficial effect on the bioactivity of peptides.
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Nongkhlaw, Fenella MW, and Santa R. Joshi. "Investigation on the bioactivity of culturable endophytic and epiphytic bacteria associated with ethnomedicinal plants." Journal of Infection in Developing Countries 9, no. 09 (September 27, 2015): 954–61. http://dx.doi.org/10.3855/jidc.4967.
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Introduction: The growing need for the bioactive compounds of ethnomedicinal plants for the treatment of diseases has resulted in exploitation of medicinal plants. The present investigation aimed to study the diversity of endophytic and epiphytic bacteria associated with ethnomedicinal plants and to explore their potential as source of bioactive compounds. Methodology: Characterization of culturable endophytic and epiphytic bacteria associated with 11 ethnomedicinal plants and their potential as natural antioxidants was assessed through free radical scavenging activity, total phenolics, total flavonoids, metal ion chelation, and antagonistic activity. Genetic screening to assess the potential of endophytes and epiphytes to synthesize bioactive compounds was achieved by screening for the presence of the non-ribosomal peptide synthetase (NRPS) gene. Result: The frequently isolated endophytic bacterium recovered was Bacillus sp. Antioxidative property of the bacterial extracts revealed endophytes with potent antioxidant activity and better antagonistic activity as compared to epiphytes. Genetic screening revealed the presence of the NRPS gene in seven plant-associated bacteria, indicating the production of natural products. Conclusions: The study indicated the extracts of bacterial endophytes associated with ethnomedicinal plants as good sources of natural products with potential application in oxidative stress. The isolates could be used as new bioactive agents.
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Kluczyk, Alicja, Julita Ludwiczak, Maciej Modzel, Mariola Kuczer, Marek Cebrat, Monika Biernat, and Remigiusz Bąchor. "Chemical and biological properties of anti-wrinkle peptide Argireline." Aesthetic Cosmetology and Medicine 10, no. 3 (June 2021): 125–33. http://dx.doi.org/10.52336/acm.2021.10.3.05.
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Argireline, a peptide with the sequence: Ac-Glu-Glu-Met-Gln-Arg-Arg-NH2, also known as Acetyl Hexapeptide-8, reduces facial lines and wrinkles by destabilization of the formation of the SNARE complex (SNAP Receptor, soluble N-ethylmaleimide sensitive factor (NSF) attachment protein receptor), thus preventing muscle contraction. It is a biosafe cosmetic alternative to the botulinum toxin. The method of choice in bioactive peptide analysis is reversed-phase high performance liquid chromatography coupled with mass spectrometry (LC-MS). The aim of this work as to present the properties of Argireline and the analysis of cosmetic products containing this peptide. Previous reports on possible Argireline transformations in cosmetic formulations have not confirmed deacetylation, whereas the oxidation of methionine residue was detected by our team. As the biological activity of the oxidized Argireline is not known, further biological studies, as well as efficient analytical procedures for transformation monitoring and quality control in cosmetic products, are necessary.