Готові списки джерел за темами / Amphibian peptides

Добірка наукової літератури з теми "Amphibian peptides"

Автор: Grafiati

Опубліковано: 10 грудня 2022

Оновлено: 28 січня 2023

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Статті в журналах з теми "Amphibian peptides"

Wang, Guangshun. "Bioinformatic Analysis of 1000 Amphibian Antimicrobial Peptides Uncovers Multiple Length-Dependent Correlations for Peptide Design and Prediction." Antibiotics 9, no. 8 (August 7, 2020): 491. http://dx.doi.org/10.3390/antibiotics9080491.

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Amphibians are widely distributed on different continents, except for the polar regions. They are important sources for the isolation, purification and characterization of natural compounds, including peptides with various functions. Innate immune antimicrobial peptides (AMPs) play a critical role in warding off invading pathogens, such as bacteria, fungi, parasites, and viruses. They may also have other biological functions such as endotoxin neutralization, chemotaxis, anti-inflammation, and wound healing. This article documents a bioinformatic analysis of over 1000 amphibian antimicrobial peptides registered in the Antimicrobial Peptide Database (APD) in the past 18 years. These anuran peptides were discovered in Africa, Asia, Australia, Europe, and America from 1985 to 2019. Genomic and peptidomic studies accelerated the discovery pace and underscored the necessity in establishing criteria for peptide entry into the APD. A total of 99.9% of the anuran antimicrobial peptides are less than 50 amino acids with an average length of 24 and a net charge of +2.5. Interestingly, the various amphibian peptide families (e.g., temporins, brevinins, esculentins) can be connected through multiple length-dependent relationships. With an increase in length, peptide net charge increases, while the hydrophobic content decreases. In addition, glycine, leucine, lysine, and proline all show linear correlations with peptide length. These correlations improve our understanding of amphibian peptides and may be useful for prediction and design of new linear peptides with potential applications in treating infectious diseases, cancer and diabetes.

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CHEN, Tianbao, Susan FARRAGHER, Anthony J. BJOURSON, David F. ORR, Pingfan RAO, and Chris SHAW. "Granular gland transcriptomes in stimulated amphibian skin secretions." Biochemical Journal 371, no. 1 (April 1, 2003): 125–30. http://dx.doi.org/10.1042/bj20021343.

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Amphibian defensive skin secretions are complex, species-specific cocktails of biologically active molecules, including many uncharacterized peptides. The study of such secretions for novel peptide discovery is time-limited, as amphibians are in rapid global decline. While secretion proteome analysis is non-lethal, transcriptome analysis has until now required killing of specimens prior to skin dissection for cDNA library construction. Here we present the discovery that polyadenylated mRNAs encoding dermal granular gland peptides are present in defensive skin secretions, stabilized by endogenous nucleic acid-binding amphipathic peptides. Thus parallel secretory proteome and transcriptome analyses can be performed without killing the specimen in this model amphibian system—a finding that has important implications in conservation of biodiversity within this threatened vertebrate taxon and whose mechanistics may have broader implications in biomolecular science.

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Cao, Xiaoqing, Jing Tang, Zhe Fu, Zhuo Feng, Siyuan Wang, Meifeng Yang, Chunyun Wu, Ying Wang, and Xinwang Yang. "Identification and Characterization of a Novel Gene-encoded Antioxidant Peptide from Odorous Frog Skin." Protein & Peptide Letters 26, no. 3 (March 15, 2019): 160–69. http://dx.doi.org/10.2174/0929866525666181114153136.

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Background: Amphibian skin plays an essential role in protecting organisms from harmful external factors such as UV radiation. How amphibians protect themselves from reactive oxygen species following long-term sun exposure is an important and interesting question. Amphibian skins possess a novel antioxidant system composed of various Antioxidant Peptides (AOPs), which maintain redox homeostasis. However, only a few AOPs have been identified so far. Methods: Using combinational methods of peptidomics and genomics, we characterized a novel gene-encoded antioxidant peptide (herein named OA-VI12) from Odorrana andersonii skin secretions, which was produced by the post-translational processing of a 59-residue prepropeptide. The amino acid sequence of the OA-V112 was 'VIPFLACRPLGL', with a molecular mass of 1298.6 Da and no observed post-transcriptional modifications. Functional analysis demonstrated that OA-VI12 was capable of scavenging ABTS+, DPPH, NO and decreasing the Fe3+ production. Results: We determined that the C7 amino acid was responsible for ABTS+ and Fe3+ scavenging, activities, the F4, C7, and P9 amino acids were crucial for DPPH scavenging activity, and the P9 amino acid was responsible for NO scavenging activity. Unlike several other amphibian peptides, OA-VI12 did not accelerate wound healing in a full-thickness skin-wound mouse model and did not demonstrate direct microbial killing. Here, we identified and named a novel gene-encoded antioxidant peptide from the skin secretions of an odorous frog species, which may assist in the development of potential antioxidant candidates. Conclusion: This study may help improve our understanding of the molecular basis of amphibians’ adaptation to environments experiencing long-term UV radiation.

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Patocka, Jiri, Eugenie Nepovimova, Blanka Klimova, Qinghua Wu, and Kamil Kuca. "Antimicrobial Peptides: Amphibian Host Defense Peptides." Current Medicinal Chemistry 26, no. 32 (November 19, 2019): 5924–46. http://dx.doi.org/10.2174/0929867325666180713125314.

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Antimicrobial Peptides (AMPs) are one of the most common components of the innate immune system that protect multicellular organisms against microbial invasion. The vast majority of AMPs are isolated from the frog skin. Anuran (frogs and toads) skin contains abundant AMPs that can be developed therapeutically. Such peptides are a unique but diverse group of molecules. In general, more than 50% of the amino acid residues form the hydrophobic part of the molecule. Normally, there are no conserved structural motifs responsible for activity, although the vast majority of the AMPs are cationic due to the presence of multiple lysine residues; this cationicity has a close relationship with antibacterial activity. Notably, recent evidence suggests that synthesis of AMPs in frog skin may confer an advantage on a particular species, although they are not essential for survival. Frog skin AMPs exert potent activity against antibiotic-resistant bacteria, protozoa, yeasts, and fungi by permeating and destroying the plasma membrane and inactivating intracellular targets. Importantly, since they do not bind to a specific receptor, AMPs are less likely to induce resistance mechanisms. Currently, the best known amphibian AMPs are esculentins, brevinins, ranacyclins, ranatuerins, nigrocin-2, magainins, dermaseptins, bombinins, temporins, and japonicins-1 and -2, and palustrin-2. This review focuses on these frog skin AMPs and the mechanisms underlying their antimicrobial activity. We hope that this review will provide further information that will facilitate further study of AMPs and cast new light on novel and safer microbicides.

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McMillan, Katelyn A. M., and Melanie R. Power Coombs. "Review: Examining the Natural Role of Amphibian Antimicrobial Peptide Magainin." Molecules 25, no. 22 (November 20, 2020): 5436. http://dx.doi.org/10.3390/molecules25225436.

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Host defense peptides (HDPs) are a group of antimicrobial peptides (AMPs) that are crucial components of the innate immune system of many different organisms. These small peptides actively kill microbes and prevent infection. Despite the presence of AMPs in the amphibian immune system, populations of these organisms are in decline globally. Magainin is an AMP derived from the African clawed frog (Xenopus laevis) and has displayed potent antimicrobial effects against a wide variety of microbes. Included in this group of microbes are known pathogens of the African clawed frog and other amphibian species. Arguably, the most deleterious amphibious pathogen is Batrachochytrium dendrobatidis, a chytrid fungus. Investigating the mechanism of action of magainin can help understand how to effectively fight off infection. By understanding amphibian AMPs’ role in the frog, a potential conservation strategy can be developed for other species of amphibians that are susceptible to infections, such as the North American green frog (Rana clamitans). Considering that population declines of these organisms are occurring globally, this effort is crucial to protect not only these organisms but the ecosystems they inhabit as well.

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Holthausen, David J., Sanil George, and Joshy Jacob. "Amphibian innate immune mediators protect against human Influenza strains." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 63.7. http://dx.doi.org/10.4049/jimmunol.196.supp.63.7.

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Abstract Frogs and toads are incredible reservoirs of biologically active peptides. Amphibians secrete host defense peptides from their skin as part of their innate immune response. This ancient response acts to protect the amphibians against microbes. The quantity and scope of these secreted peptides dwarfs mammalian analogues, accounting for a substantial portion of all known host defense peptides. The non-invasive and non-harmful methods for frog peptide collection, in tandem with the abundance and breadth of these peptides, makes them excellent choices for novel peptide drug therapies. Studies have shown that these peptides can effectively neutralize enveloped viruses, mycobacteria, gram-negative and gram-positive bacteria, fungi, and even cancerous or transformed cells. Because of the nature of antimicrobial peptides, often targeting the most critical, conserved aspects of a micro-organism, they may prove a vital alternative to conventional drugs plagued by pathogen resistance. Given this untapped potential for anti-viral therapies, we assessed novel host defense peptides from the skin of the Indian fungoid frog, Hylarana malabarica. During our analysis, we isolated several peptides from H. malabarica that show anti-viral activity against human influenza viruses. Our studies indicate that peptides from H. malabarica demonstrate anti-influenza activity in vitro, and also show potential as an anti-viral therapy in vivo.

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Yang, Jie, Chengliang Tong, Junmei Qi, Xiaoying Liao, Xiaokun Li, Xu Zhang, Mei Zhou, et al. "Engineering and Structural Insights of a Novel BBI-like Protease Inhibitor Livisin from the Frog Skin Secretion." Toxins 14, no. 4 (April 12, 2022): 273. http://dx.doi.org/10.3390/toxins14040273.

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The Bowman–Birk protease inhibitor (BBI) family is a prototype group found mainly in plants, particularly grasses and legumes, which have been subjected to decades of study. Recently, the discovery of attenuated peptides containing the canonical Bowman–Birk protease inhibitory motif has been detected in the skin secretions of amphibians, mainly from Ranidae family members. The roles of these peptides in amphibian defense have been proposed to work cooperatively with antimicrobial peptides and reduce peptide degradation. A novel trypsin inhibitory peptide, named livisin, was found in the skin secretion of the green cascade frog, Odorrana livida. The cDNA encoding the precursor of livisin was cloned, and the predicted mature peptide was characterized. The mature peptide was found to act as a potent inhibitor against several serine proteases. A comparative activity study among the native peptide and its engineered analogs was performed, and the influence of the P1 and P2′ positions, as well as the C-terminal amidation on the structure–activity relationship for livisin, was illustrated. The findings demonstrated that livisin might serve as a potential drug discovery/development tool.

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Ramsey, Jeremy P., Laura K. Reinert, Laura K. Harper, Douglas C. Woodhams, and Louise A. Rollins-Smith. "Immune Defenses against Batrachochytrium dendrobatidis, a Fungus Linked to Global Amphibian Declines, in the South African Clawed Frog, Xenopus laevis." Infection and Immunity 78, no. 9 (June 28, 2010): 3981–92. http://dx.doi.org/10.1128/iai.00402-10.

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ABSTRACT Batrachochytrium dendrobatidis is a chytrid fungus that causes the lethal skin disease chytridiomycosis in amphibians. It is regarded as an emerging infectious disease affecting diverse amphibian populations in many parts of the world. Because there are few model amphibian species for immunological studies, little is known about immune defenses against B. dendrobatidis. We show here that the South African clawed frog, Xenopus laevis, is a suitable model for investigating immunity to this pathogen. After an experimental exposure, a mild infection developed over 20 to 30 days and declined by 45 days postexposure. Either purified antimicrobial peptides or mixtures of peptides in the skin mucus inhibited B. dendrobatidis growth in vitro. Skin peptide secretion was maximally induced by injection of norepinephrine, and this treatment resulted in sustained skin peptide depletion and increased susceptibility to infection. Sublethal X-irradiation of frogs decreased leukocyte numbers in the spleen and resulted in greater susceptibility to infection. Immunization against B. dendrobatidis induced elevated pathogen-specific IgM and IgY serum antibodies. Mucus secretions from X. laevis previously exposed to B. dendrobatidis contained significant amounts of IgM, IgY, and IgX antibodies that bind to B. dendrobatidis. These data strongly suggest that both innate and adaptive immune defenses are involved in the resistance of X. laevis to lethal B. dendrobatidis infections.

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VanCompernolle, Scott E., R. Jeffery Taylor, Kyra Oswald-Richter, Jiyang Jiang, Bryan E. Youree, John H. Bowie, Michael J. Tyler, et al. "Antimicrobial Peptides from Amphibian Skin Potently Inhibit Human Immunodeficiency Virus Infection and Transfer of Virus from Dendritic Cells to T Cells." Journal of Virology 79, no. 18 (September 15, 2005): 11598–606. http://dx.doi.org/10.1128/jvi.79.18.11598-11606.2005.

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ABSTRACT Topical antimicrobicides hold great promise in reducing human immunodeficiency virus (HIV) transmission. Amphibian skin provides a rich source of broad-spectrum antimicrobial peptides including some that have antiviral activity. We tested 14 peptides derived from diverse amphibian species for the capacity to inhibit HIV infection. Three peptides (caerin 1.1, caerin 1.9, and maculatin 1.1) completely inhibited HIV infection of T cells within minutes of exposure to virus at concentrations that were not toxic to target cells. These peptides also suppressed infection by murine leukemia virus but not by reovirus, a structurally unrelated nonenveloped virus. Preincubation with peptides prevented viral fusion to target cells and disrupted the HIV envelope. Remarkably, these amphibian peptides also were highly effective in inhibiting the transfer of HIV by dendritic cells (DCs) to T cells, even when DCs were transiently exposed to peptides 8 h after virus capture. These data suggest that amphibian-derived peptides can access DC-sequestered HIV and destroy the virus before it can be transferred to T cells. Thus, amphibian-derived antimicrobial peptides show promise as topical inhibitors of mucosal HIV transmission and provide novel tools to understand the complex biology of HIV capture by DCs.

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Xiao, Yao, Cunbao Liu, and Ren Lai. "Antimicrobial peptides from amphibians." BioMolecular Concepts 2, no. 1-2 (April 1, 2011): 27–38. http://dx.doi.org/10.1515/bmc.2011.006.

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AbstractIncreased prevalence of multi-drug resistance in pathogens has encouraged researchers to focus on finding novel forms of anti-infective agents. Antimicrobial peptides (AMPs) found in animal secretions are components of host innate immune response and have survived eons of pathogen evolution. Thus, they are likely to be active against pathogens and even those that are resistant to conventional drugs. Many peptides have been isolated and shown to be effective against multi-drug resistant pathogens. More than 500 AMPs have been identified from amphibians. The abundance of AMPs in frog skin is remarkable and constitutes a rich source for design of novel pharmaceutical molecules. Expression and post-translational modifications, discovery, activities and probable therapeutic application prospects of amphibian AMPs will be discussed in this article.

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Дисертації з теми "Amphibian peptides"

Wegener, Kate Louise. "Amphibian peptides : their structures and bioactivity." Title page, contents and abstract only, 2001. http://web4.library.adelaide.edu.au/theses/09PH/09phw4114.pdf.

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Copies of author's previously published works inserted. Bibliography: leaves 237-268. The skin secretion of the northern Australian frog Litoria dahlii was investigated, with eleven novel peptides identified. These peptides have moderate biological activity, including antibacterial and anticancer actions, as well as the capacity to inhibit the enzyme neuronal nitric oxide synthase. Many potent broad-spectrum antibiotics have been isolated from Australian amphibians, and are believed to act by disrupting the bacterial cell membrane by forming transmembrane 'barrel-stave' type ion channels, lipid-incorporating toroidal pores or by assembling as a 'carpet' over the mebrane surface. The structures of several antibacterial peptides were determined using nuclear magnetic resonance spectroscopy and restrained molecular dynamics calculations. Experimental results suggest these peptides operate by the 'carpet' mechanism.

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Salmon, Amanda Lizabeth. "Structural and functional characterisation of bioactive amphibian skin peptides." Thesis, Queen's University Belfast, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.247347.

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Shi, Daning. "Functional studies on the peptides from amphibian skin secretions." Thesis, Queen's University Belfast, 2016. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.711901.

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Therapeutic peptides are continuing to grow in prominence among pharmaceutical manufacturers. Drugs based on peptides offer lower toxicity, show higher specificity, and demonstrate fewer toxicology issues than small molecule drugs. The specificity of peptides has tremendous clinical value and makes them very attractive and potentially lucrative therapeutics. In order to protect themselves from a great variety of potential predators, amphibians have evolved different morphological, physiological and behavioural features. One such defence mechanism is the secretion from granular skin glands. Frogs and toads have two different types of skin glands -mucous and granular. The mucous glands are present throughout the skin and their secretion provides a moist coating that is necessary for cutaneous respiration. The granular glands may be distributed across the body but are often concentrated around the head or neck and are usually activated by stress or injury. Secretions from these glands are complex, species-specific cocktails of bioactive molecules, including peptides. The Chinese have perhaps the most advanced and temporally tested system of natural therapies among traditional medicines and therapeutics have been derived from both plants and animals, including amphibians. This study focuses on the vast potential of natural peptide libraries contained in amphibian skin secretions as a source of novel drug candidates for conditions such as hypertension, cancer, and bacterial infection.

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Wang, Ran. "Biological effects of novel amphibian skin peptides and their catabolism." Thesis, Queen's University Belfast, 2012. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.557850.

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Amphibian skin secretions are known to contain numerous peptides with a large array of biological activities. Among the anuran amphibians, the Neotropical hylid frogs belonging to the subfamily Phyllomedusinae, are an excellent source of such bioactive peptides with antimicrobial and pharmacological activities. To date, more than 200 peptides from this frog taxon have been reported in the scientific literature and their structures have been deposited in genomic and proteomic data banks such as the Universal Protein Resource Consortium (UniProt). In this thesis, we have identified four novel tryptophyllins (TPHs) from the skin secretions of four different phyllomedusine species (Phyllomedusa sauvagei, Phyllomedusa hypocondrialis, Agalyehnis eallidryas and Phyllomedusa bieolor). The primary structures of these peptides were determined by combinations of Edman degradation and mass spectrometry techniques. Molecular cloning of respective cDNA sequences encoding the precursors of these TPHs was achieved from skin cDNA libraries of each species. The amino acid sequences deduced from the nucleotide sequences of cloned precursor cDNAs corresponded exactly with those obtained by chemical/mass spectrometric techniques. Some of these novel TPH peptides were found to have potent effects on mammalian smooth muscle and here we report for the first time that TPHs can antagonise the bradykinin-induced relaxation responses in rat tail artery smooth muscle preparations and that they have anticancer effects on human prostate cancer (LNCaPIPC3IDU145) cell lines. The catabolism of these TPHs by prostate cancer cells was analysed and all were found to be highly-resistant to degradation under the experimental conditions employed. The polyadenylated mRNAs encoding both bradykinin receptor subtypes, Bland B2, were also shown to be expressed in all three prostate cancer cell lines through molecular cloning of specific receptor cDNA fragments from cDNA libraries constructed from each. These data suggest that bradykinin receptors could be a hitherto uninvestigated target of potential utility in the treatment of prostate cancer. The data generated through the discrete studies reported in this thesis may aid in the understanding of possible biological roles played by amphibian skin TPHs and the contributions made by specific structural features within this heterogenous and largely unstudied family of amphibian skin peptides. The peptides described here for the first time may represent novel lead compounds for the design/development of new therapeutics for human neoplastic disease.

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Gao, Yitian. "Peptidomic and bioinformatic studies on bioactive peptides from amphibian skin secretions." Thesis, Queen's University Belfast, 2017. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.726351.

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Phyllomedusa, as a significant genus of South American and Neotropical hylid frogs, has been researched for several years and this has produced abundant bioactive peptides. Most frog species have poisonous skin secretions that can act as a defence against potential predators and pathogens. Therefore, Phyllomedusa frogs have been referred to as a "treasure store” and compared to be the most promising drug sources. Antimicrobial peptides (AMPs), as the most widely isolated group of peptides from skin secretions of Phyllomedusa frogs, have been considered as a novel therapeutic approach to address the serious difficulties in treating antibiotic resistant infections. In addition to their direct antimicrobial activities, AMPs can regulate innate immune responses and can facilitate wound healing and angiogenesis. Phylloseptins are a family of potent AMPs that are widely distributed in the skin secretions of phyllomedusine frogs. The structures of these peptides are relatively conserved, containing 19-21 amino acids with C-terminal amidation, a cationic amphiphilic structure and an a-helical domain. Medusins are a recently discovered family of AMPs in the Phyllomedusinae, with highly-conserved sequences and relatively strong antimicrobial activity against Gram-positive bacteria and fungi, but without obvious cytotoxicity against eukaryotic cells at effective antibacterial concentrations. Dermaseptins are one of the most significant families of amphibian host defence peptides that are usually cationic, contain 10-50 amino acids and inhibit the growth of a wide range of microbes. Here, we report novel peptides from the skin secretion of the Phyllomedusa frogs,Phyllomedusa tarsius and Phyllomedusa sauvagii, identified using a high throughput method combining molecular cloning with mass spectrometry to establish their primary structures. A phylloseptin peptide, a medusin peptide and two dermaseptin peptide-precursor-encoding cDNAs were cloned from defensive skin secretion-derived cDNA libraries by a rapid amplification of cDNA ends technique. R6verse-phase HPLC and tandem mass spectrometry confirmed the presence and primary structure of mature peptide sequences. The secondary structure and physicochemical parameters of each peptide were predicted with using a predictive software system. Cationicity- and amphipathicity- enhanced analogues of the phylloseptin and medusin were by engineered through amino acid substitutions by computational modelling. The synthetic peptides displayed varying degrees of activities. Phylloseptin was active against Staphylococcus aureus and Candida albicans and medusin only against Staphylococcus aureus. However, cationicity-enhanced peptides displayed significant increases in potency and broader spectra of antimicrobial activities. In addition, the appearance of activity against antibiotic-resistant MRSA and biofilms was observed after modification of the structures. Both D-substituted analogues of phylloseptin and medusin showed potent antimicrobial activities as well as stable functional efficiency in the serum. Two dermaseptin peptides exhibited high inhibition against multiple tested microorganisms and a range of cancer cells. These data provide evidence thatAMPs may be candidates as novel antibiotic leads and that targeted modification of a natural AMP template can provide new insights into antibiotic design and development.

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Lv, Liangchun. "Peptidomic and genomic analyses on bioactive peptides from the amphibian skin." Thesis, Queen's University Belfast, 2017. https://pure.qub.ac.uk/portal/en/theses/peptidomic-and-genomic-analyses-on-bioactive-peptides-from-the-amphibian-skin(ffa8be66-4a1e-404f-b22a-3f6fbb4782b5).html.

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Amphibian skin can secrete mucus from skin glands and this mucus always contains many types of antimicrobial peptides (AMPs) which can protect the hosts from bacterial infection. AMPs have been studied for a few decades with significant results as increasing numbers have been found, explored and developed to be evaluated as clinical drugs. This is a huge source of new molecules to help humans in their fight against diseases. In Chapter 3, a phylloxin-like AMP, QUB1966 and its analogue QUB2260, were studied. The results showed that QUB1966 exhibited antimicrobial effects against Gram-positive (Staphylococcus aureus) bacteria, Gram-negative (Escherichia coli) bacteria and yeast (Candida albicans). The modification increased the positive charge of the AMP, which enhanced the interaction between the peptide and the membrane of the selected microbes. The results showed that the modified peptide, QUB2260, expressed more potent antimicrobial function than the wild-type peptide QUB1966, increasing its inhibitory effect by 32-fold against E. coli and C. albicans, and 4-fold against S. aureus. Thus, the modified peptide might provide favourable prospects for novel biomedicine design and antibiotics substitution. In Chapter 4, a bradykinin-related peptide (BRP), QUB1315 (RAA-Val1, Thr6-bradykinin), was isolated from the skin secretion of Odorrana schmackeri with the defined primary sequence of RAAVPPGFTPFR. After bioactivity studies, QUB1351 revealed a dose-dependent contractile property on rat bladder. The analogue peptide, QUB1281 (RAA-Val1, Thr6, Leu8-bradykinin), was modified based on QUB1315 by replacing a single amino acid from Phe8 to Leu8 to test the antagonistic activity. However, the results showed that the modified peptide, QUB1281, was still an agonist. QUB1281 expressed less potency on bladder contraction than the wild-type QUB1315. It was also found that Thr6 and Leu8 might contribute to agonist effects and the substitution at position 8 could affect the affinity between peptides and bradykinin receptors. In Chapter 5, two novel peptides from Odorrana schmackeri, QUB1517 and QUB2025, were found to exhibit antibacterial potency against Gram-positive (Staphylococcus aureus) bacteria, Gram-negative (Escherichia coli) bacteria and yeast (Candida albicans). Their similar antimicrobial effects against these three microbes assumed that the same sequence domain might contribute to the antimicrobial activity. However, they both showed higher inhibitory activity on Gram-positive bacteria than Gram-negative bacteria. It is expected that the novel data described in this thesis will contribute to the burgeoning database of biologically-active peptides from amphibian skin secretions and may ultimately provide a basis for the development of new classes of peptide drugs for both major diseases and for orphan indications.

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Zheng, Huiru. "New algorithms for the analysis of mass spectral profiles from amphibian data." Thesis, University of Ulster, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.272069.

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Chia, Brian Cheng San. "Amphibian antimicrobial peptides : their structures and mechanisms of action : a thesis presented for the degree of Doctor of Philosophy." Title page, contents and abstract only, 2000. http://web4.library.adelaide.edu.au/theses/09PH/09phc532.pdf.

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Copy of author's previously published works inserted. Bibliography: leaves 183-220. Three antimicrobial peptides, maculatin 1.1, uperin 3.6 and caerin 4.1 have been isolated from the respective skin glands of the Australian amphibians Litoria genimaculata, Uperoleia mjobergii and Litoria caerulea. To gain a deeper insight into their mechanisms of action, three dimensional structural studies have been conducted using circular dichroism, two-dimensional nuclear resonance and computer modelling techniques. The role of central flexibility within antibiotic peptides in their interaction with bacterial membranes is also discussed.

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Wabnitz, Paul Andrew. "Chemistry and medical implications of novel amphibian peptides : a thesis submitted for the degree of Doctor of Philosophy /." Title page, contents and abstract only, 1999. http://web4.library.adelaide.edu.au/theses/09PH/09phw112.pdf.

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Brinkworth, Craig Steven. "The primary and secondary structure determination of bioactive amphibian peptides : a thesis submitted for the degree of Doctor of Philosophy." Title page, contents and abstract only, 2003. http://web4.library.adelaide.edu.au/theses/09PH/09phb8586.pdf.

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"May 2003." Includes a list of publications by the author (journal articles related to thesis); and , copies of journal articles co-authored by the author. Includes bibliographical references (leaves 226-242) The solution structures of three peptides: Ala4Lys14-citopin 1.1 (amphipathic đ-helix); Gly15Gly19-caerin 1.1 (a less defined đ-helix); and, frenatin 3.1 (amphipathic đ-helix with a flexible c-terminal end) are presented in a discussion about structure/activity relationship

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Книги з теми "Amphibian peptides"

International Symposium on Nonmammalian Peptides (1st 1985 Rome, Italy). First International Symposium on Nonmammalian Peptides: Held in Rome, Italy, May 11-15, 1985 at Accademia Nazionale dei Lincei, honorary president Vittorio Erspamer. Polifarma, Roma: Universitá degli Studi di Roma, 1985.

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Farragher, Susan. Study of peptide transcripts in the skin and stimulated skin secretions of three different species of amphibians. [S.l: The author], 2002.

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Частини книг з теми "Amphibian peptides"

Erspamer, Vittorio. "Peptides, Amphibian (Skin)." In Comparative Neuroscience and Neurobiology, 104–6. Boston, MA: Birkhäuser Boston, 1988. http://dx.doi.org/10.1007/978-1-4899-6776-3_42.

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Lovas, Sandor, Yunxia Wang, Finbarr O’Harte, Tim Badgery-Parker, Nicholas Chartrel, Hubert Vaudry, Elizabeth Burcher, D. David Smith, Richard F. Murphy, and J. Michael Conlon. "Isolation, synthesis and binding properties of novel amphibian tachykinins." In Peptides 1992, 669–70. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1470-7_304.

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Negri, Lucia. "Amphibian Opioids: Novel Dermorphin-Like Peptides." In Growth Factors, Peptides and Receptors, 51–60. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2846-3_6.

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Negri, Lucia, and Roberta Lattanzi. "Opioid Peptides from the Amphibian Skin." In Encyclopedia of Pain, 2432–36. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-28753-4_2959.

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Acher, R., J. Chauvet, G. Michel, and Y. Rouillé. "Hydrins, hydroosmotic neurohypophysial peptides involved in neuroendocrine control of amphibian water homeostasis through specific receptors." In Peptides, 834–36. Dordrecht: Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-011-0683-2_279.

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Kreil, Günther. "Antimicrobial Peptides from Amphibian Skin: An Overview." In Ciba Foundation Symposium 186 - Antimicrobial Peptides, 77–90. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470514658.ch5.

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Sagan, Sandrine, Stéphane Charpentier, Mohammed Naïm, Antoine Delfour, and Pierre Nicolas. "Opioid peptides from amphibian skin: Contribution of the amino acids of the ‘address’ domain to the δ-selectivity of dermenkephalin." In Peptides 1992, 645–46. Dordrecht: Springer Netherlands, 1993. http://dx.doi.org/10.1007/978-94-011-1470-7_292.

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Conlon, J. Michael, and Jérôme Leprince. "Identification and Analysis of Bioactive Peptides in Amphibian Skin Secretions." In Methods in Molecular Biology, 145–57. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-535-4_12.

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Lai, Ren. "Combined Peptidomics and Genomics Approach to the Isolation of Amphibian Antimicrobial Peptides." In Methods in Molecular Biology, 177–90. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-535-4_14.

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Wang, Guangshun. "Structural Analysis of Amphibian, Insect, and Plant Host Defense Peptides Inspires the Design of Novel Therapeutic Molecules." In Host Defense Peptides and Their Potential as Therapeutic Agents, 229–52. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-32949-9_9.

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Mangoni, Maria Luisa, Floriana Cappiello, Bruno Casciaro, Chen Chen, Debarun Dutta, Alison McDermott, Mark Dp Willcox, and Peter Di. "How to control Pseudomonas aeruginosa-induced pneumoniaand keratitis? A lesson from the amphibian skin-derived peptide Esculentin(1-21) and its diastereomer." In 35th European Peptide Symposium. Prompt Scientific Publishing, 2018. http://dx.doi.org/10.17952/35eps.2018.228.

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