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NEVALAINEN, Leena T., Takashi AOYAMA, Mitsuhiko IKURA, Anna CRIVICI, Hong YAN, Nam-Hai CHUA, and Angus C. NAIRN. "Characterization of novel calmodulin-binding peptides with distinct inhibitory effects on calmodulin-dependent enzymes." Biochemical Journal 321, no. 1 (January 1, 1997): 107–15. http://dx.doi.org/10.1042/bj3210107.
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We describe the isolation and interaction with calmodulin (CaM) of two 10-amino-acid peptides (termed peptides 1 and 2; AWDTVRISFG and AWPSLQAIRG respectively) derived from a phage random peptide display library. Both peptides are shorter than previously described CaM-binding peptides and lack certain features found in the sequences of CaM-binding domains present in CaM-activated enzymes. However, 1H NMR spectroscopy and fluorimetry indicate that both peptides interact with CaM in the presence of Ca2+. The two peptides differentially inhibited CaM-dependent kinases I and II (CaM kinases I and II) but did not affect CaM-dependent phosphodiesterase. Peptide 1 inhibited CaM kinase I but not CaM kinase II, whereas peptide 2 inhibited CaM kinase II, but only partially inhibited CaM kinase I at a more than 10-fold higher concentration. Peptide 1 also inhibited a plant calcium-dependent protein kinase, whereas peptide 2 did not. The ability of peptides 1 and 2 to differentially inhibit CaM-dependent kinases and CaM-dependent phosphodiesterase suggests that they may bind to distinct regions of CaM that are specifically responsible for activation of different CaM-dependent enzymes.
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Srivastava, Mrinal Ranjan, Farzana Mahdi, Abbas Ali Mahdi, Sharique Ahmad, and Anu Chandra. "BIOLOGICAL EFFECTS OF C-PEPTIDE AND PROINSULIN: WE JIBE TOGETHER." Era's Journal of Medical Research 6, no. 1 (June 2019): 103–9. http://dx.doi.org/10.24041/ejmr2019.115.
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Lorenzón, E. N., G. F. Cespedes, E. F. Vicente, L. G. Nogueira, T. M. Bauab, M. S. Castro, and E. M. Cilli. "Effects of Dimerization on the Structure and Biological Activity of Antimicrobial Peptide Ctx-Ha." Antimicrobial Agents and Chemotherapy 56, no. 6 (March 5, 2012): 3004–10. http://dx.doi.org/10.1128/aac.06262-11.
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ABSTRACTIt is well known that cationic antimicrobial peptides (cAMPs) are potential microbicidal agents for the increasing problem of antimicrobial resistance. However, the physicochemical properties of each peptide need to be optimized for clinical use. To evaluate the effects of dimerization on the structure and biological activity of the antimicrobial peptide Ctx-Ha, we have synthesized the monomeric and three dimeric (Lys-branched) forms of the Ctx-Ha peptide by solid-phase peptide synthesis using a combination of 9-fluorenylmethyloxycarbonyl (Fmoc) andt-butoxycarbonyl (Boc) chemical approaches. The antimicrobial activity assay showed that dimerization decreases the ability of the peptide to inhibit growth of bacteria or fungi; however, the dimeric analogs displayed a higher level of bactericidal activity. In addition, a dramatic increase (50 times) in hemolytic activity was achieved with these analogs. Permeabilization studies showed that the rate of carboxyfluorescein release was higher for the dimeric peptides than for the monomeric peptide, especially in vesicles that contained sphingomyelin. Despite different biological activities, the secondary structure and pore diameter were not significantly altered by dimerization. In contrast to the case for other dimeric cAMPs, we have shown that dimerization selectively decreases the antimicrobial activity of this peptide and increases the hemolytic activity. The results also show that the interaction between dimeric peptides and the cell wall could be responsible for the decrease of the antimicrobial activity of these peptides.
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Wigle, D. A., B. M. Bennett, D. B. Jennings, I. R. Sarda, T. G. Flynn, and S. C. Pang. "Biological effects of rat iso-atrial natriuretic peptide and brain natriuretic peptide are indistinguishable from each other." Canadian Journal of Physiology and Pharmacology 70, no. 11 (November 1, 1992): 1525–28. http://dx.doi.org/10.1139/y92-218.
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Rat brain natriuretic peptide (rBNP) and iso-atrial natriuretic peptide (iso-rANP) were discovered independently by two research laboratories. They are considered to be members of the B-type natriuretic peptides. Except for the Gln/Leu substitution at position 44, the amino acid sequence of iso-rANP is identical with that of the C-terminal 45 amino acids of rat pro-BNP and with the 5-kDa cardiac peptide from rat atria. To determine whether this amino acid substitution can modify the known biological effects of rBNP and iso-rANP, the present investigation examined the cardiovascular and renal responses, vasorelaxant effect, receptor binding characteristics, and cyclic GMP production by the two peptides in relation to that of rat atrial natriuretic peptide (rANP). Results indicate that rBNP and iso-rANP are indistinguishable from each other in terms of these known biological activities of atrial natriuretic peptide. We therefore conclude that rBNP and iso-rANP are identical peptides and that the amino acid substitution at position 44 represents a polymorphic form of the rat B-type natriuretic peptide.Key words: atrial natriuretic peptide, brain natriuretic peptide, cardiovascular response, vasorelaxation, cyclic GMP, receptor binding.
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Ano, Yasuhisa, Yuka Yoshino, Kazuyuki Uchida, and Hiroyuki Nakayama. "Preventive Effects of Tryptophan–Methionine Dipeptide on Neural Inflammation and Alzheimer’s Pathology." International Journal of Molecular Sciences 20, no. 13 (June 29, 2019): 3206. http://dx.doi.org/10.3390/ijms20133206.
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Preventive approaches for age-related memory decline and dementia have become a high priority in the aging society because of the lack of therapeutic approaches. Recent epidemiological studies have reported that fermented dairy products can help prevent dementia. Previously, we identified tryptophan–tyrosine (WY) and tryptophan–methionine (WM) peptides as the suppressants of activation of the primary microglia and showed that WY peptide consumption suppresses inflammation in the brains of Alzheimer’s disease model mice. However, the effects of the WM peptide on inflammation in the brain and Alzheimer’s pathology have not been investigated. Here, we evaluated the effect of WM peptide consumption on Alzheimer’s disease model (5×FAD) mice. In 5×FAD mice, intake of WM peptide suppressed the production of inflammatory cytokines, activation of microglia, and infiltration of activated microglia around β amyloid (Aβ) depositions. WM peptide intake reduced Aβ deposition in the cortex and hippocampus and then improved the object recognition memory. Taken together with previous reports, the current findings indicate that ingestion of tryptophan-related peptides or food material rich in tryptophan-related peptides, thereby regulating microglial activity, represents a potential preventive approach for cognitive decline and dementia related to inflammation.
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Nongonierma, Alice B., and Richard J. FitzGerald. "Utilisation of the isobole methodology to study dietary peptide–drug and peptide–peptide interactive effects on dipeptidyl peptidase IV (DPP-IV) inhibition." Food & Function 6, no. 1 (2015): 312–19. http://dx.doi.org/10.1039/c4fo00883a.
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Chauhan, Sweeny, Sean O’Callaghan, Audrey Wall, Tomasz Pawlak, Ben Doyle, Alessandro Adelfio, Sanja Trajkovic, Mark Gaffney, and Nora Khaldi. "Using Peptidomics and Machine Learning to Assess Effects of Drying Processes on the Peptide Profile within a Functional Ingredient." Processes 9, no. 3 (February 26, 2021): 425. http://dx.doi.org/10.3390/pr9030425.
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Bioactive peptides are known to have many health benefits beyond nutrition; yet the peptide profile of high protein ingredients has been largely overlooked when considering the effects of different processing techniques. Therefore, to investigate whether drying conditions could affect the peptide profile and bioactivity within a functional ingredient, we examined the effects of spray (SD) and freeze (FD) drying on rice natural peptide network (NPN), a characterised functional ingredient sourced from the Oryza sativa proteome, which has previously been shown to effectively modulate circulating cytokines and improve physical performance in humans. In the manufacturing process, rice NPN was either FD or SD. Employing a peptidomic approach, we investigated the physicochemical characteristics of peptides common and unique to FD and SD preparations. We observed similar peptide profiles regarding peptide count, amino acid distribution, weight, charge, and hydrophobicity in each sample. Additionally, to evaluate the effects of drying processes on functionality, using machine learning, we examined constituent peptides with predicted anti-inflammatory activity within both groups and identified that the majority of anti-inflammatory peptides were common to both. Of note, key bioactive peptides validated within rice NPN were recorded in both SD and FD samples. The present study provides an important insight into the overall stability of the peptide profile and the use of machine learning in assessing predicted retention of bioactive peptides contributing to functionality during different types of processing.
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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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Burkitt, William I., Anastassios E. Giannakopulos, Foteini Sideridou, Sajid Bashir, and Peter J. Derrick. "Discrimination Effects in MALDI-MS of Mixtures of Peptides—Analysis of the Proteome." Australian Journal of Chemistry 56, no. 5 (2003): 369. http://dx.doi.org/10.1071/ch02155.
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Peptide ion suppression in matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) can hinder the detection of site-specific post-translational protein modifications. Within a peptide mixture, the presence or absence of a particular peptide can affect the ion intensities of other peptides in the mixture. These effects have been studied using equimolar solutions of target peptides and observation of the increase or decrease in ion intensity of the peptides upon the removal or addition of individual peptides. Gas-phase basicities and hydrophobicity measures have been used to rationalize this behaviour. ZipTips have been used to remove impurities and reduce the number of peptides present at any moment in a solution, a procedure that results in a significant increase in the total percentage of the amino acid coverage of enzymatically digested proteins. The efficacy of this approach was demonstrated using specifically nitrated lysozyme and specifically nitrated myoglobin.
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Li, Mingjie, Eric Sanchez, Jennifer Li, Cathy S. Wang, Jing Shen, Mengyin Hu, Crystal Leung, et al. "TRAF6-Dominant Negative Peptides Show Potent Inhibitory Effects On Multiple Myeloma, Osteoclast Formation and Bone Resorption." Blood 114, no. 22 (November 20, 2009): 611. http://dx.doi.org/10.1182/blood.v114.22.611.611.
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Abstract Abstract 611 Tumor necrosis factor receptor-associated factor 6 (TRAF6) has been implicated in regulating NF-κB and JNK signal transduction pathway resulting in inhibition of tumor cell proliferation and osteoclast formation. The unique biological function of TRAF6 is largely determined within its TRAF-C domain which does not interact with peptide motifs that are recognized by other TRAFs including 1, 2, 3 or 5. We have recently reported inhibition of cell proliferation and increased apoptosis of multiple myeloma (MM) cells through regulation of the NF-κB and JNK pathways through silencing the TRAF6 C-domain mRNA. In this study, we determined the effects of TRAF6 dominant negative peptides on MM cells, osteoclast formation and bone resorption. We cloned a 167 amino acid (in residues 333 to 508) fragment to produce a TRAF6 negative dominant (TRAF6dn) construct and synthesized an inhibitory decoy peptide of the TRAF6 interaction domain with CD40 and another peptide interacting with the TRAF6-RANK binding domain as well as a control peptide. All peptides were synthesized with a 16 amino acid permeable peptide. Using the MM1s, RPMI8226, and U266, we evaluated the effects of these peptides on MM tumor cell growth using an MTS assay and apoptosis with an Annexin V assay. We found that TRAF6dn peptides significantly inhibited MM cell proliferation maximally at 72 hours whereas effects on induction of apoptosis in MM cells were most prominent at 48 hours. The decrease in cell proliferation and increase in cell apoptosis occurred in a concentration-dependent fashion. We found that TRAF6dn also markedly inhibited osteoclast cell formation from freshly derived human monocytes induced by RANKL and M-CSF in a concentration-dependent fashion comparing with cells exposed to control peptide. We further examined the effects on MM cell apoptosis of the TRAF6 decoy or CD40 decoy peptides alone and in cells exposed to the combination of both peptides. The results showed either decoy peptide alone slightly induced apoptosis of MM tumor cells whereas the combination of both peptides demonstrated marked apoptosis of MM cells. We also showed that although melphalan alone induced apoptotic cell death, this effect was markedly enhanced when this alkylating agent was combined with the TRAF6 decoy peptide. Although the CD40 peptide alone did not inhibit osteoclast formation, TRAF6 decoy peptide alone and the combination of both decoy peptides markedly inhibited formation of these bone resorbing cells. We also examined the effects of TRAF6dn on NF-κB and JNK by measuring JUN kinase kinase (JNKK), which activates the MAP kinase homologues SAPK and JNK in response to IL-1 receptor stimulation. Phospho-NF-κB protein levels and phosphorylation of JNKK are both markedly reduced when MM cells are exposed to TRAF6dn fragment or TRAF6 decoy peptide. These studies suggest that TRAF6dn or the combination of TRAF6 decoy and CD40 decoy peptides may be excellent targets to block both myeloma cell and osteoclast cell formation. The study has been extended to assess the effects of these peptides in vivo using our SCID-hu murine model of human myeloma. Disclosures: No relevant conflicts of interest to declare.
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VILLA, Giorgio LA, Massimo MANNELLI, Chiara LAZZERI, Sabrina VECCHIARINO, Maria Laura DE FEO, Cristina TOSTI GUERRA, Renzo BANDINELLI, Marco FOSCHI, and Franco FRANCHI. "Different effects of atrial and C-type natriuretic peptide on the urinary excretion of endothelin-1 in man." Clinical Science 95, no. 5 (November 1, 1998): 595–602. http://dx.doi.org/10.1042/cs0950595.
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1.Following the observation that brain natriuretic peptide enhances the urinary excretion rate of endothelin-1, the relationship between natriuretic peptides and urinary endothelin-1 was further investigated. Six healthy volunteers received, on three different occasions, increasing doses of atrial or C-type natriuretic peptide (0, 2 and 4 ;pmol·min-1·kg-1 for 1 ;h each), or placebo. 2.Atrial natriuretic peptide caused significant increases in the urinary excretion of cGMP, sodium and endothelin-1, without affecting plasma endothelin-1, renal plasma flow, glomerular filtration rate and urine flow rate. C-type natriuretic peptide did not modify any of these parameters. During atrial natriuretic peptide infusion, urinary endothelin-1 directly correlated with plasma atrial natriuretic peptide, urinary cGMP and sodium excretion. 3.These results indicate that enhancement of the urinary excretion of endothelin-1 by natriuretic peptides is dose-dependent and somewhat related to their ability to bind to natriuretic peptide receptors A, activate guanylate cyclase and induce a natriuretic response.
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Drazen, J. M., S. A. Shore, and N. P. Gerard. "Substance P-induced effects in guinea pig lungs: effects of thiorphan and captopril." Journal of Applied Physiology 66, no. 3 (March 1, 1989): 1364–72. http://dx.doi.org/10.1152/jappl.1989.66.3.1364.
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The effects of the neutral metalloendopeptidase inhibitor, thiorphan, and the angiotensin-converting enzyme inhibitor, captopril, on the changes in airway opening pressure (PaO), pulmonary arterial pressure (Ppa), and weight induced by intravascular administration of substance P were examined in isolated perfused and ventilated guinea pig lungs. Administration of 1 nmol substance P without enzyme inhibitors resulted in a significant (P less than 0.01) increase in the peak PaO during ventilation from 12.4 +/- 0.5 to 22.4 +/- 2.2 cmH2O; there were small statistically insignificant increases in Ppa. The changes in PaO peaked approximately 30 s after peptide infusion and returned to preinfusion values by 5 min. In the presence of combined thiorphan (5.6 microM) and captopril (7.7 microM) the magnitude of the Pao response at 30 s (41.5 +/- 3.8 cmH2O) and at 5 min (40.0 +/- 3.6 cmH2O) after peptide infusion was significantly greater than in control lungs (P less than 0.05). The effects of substance P on PaO in the presence of the various inhibitors were not related to amount of peptide recovered in the lung effluent. Reverse-phase high-performance liquid chromatographic analysis of [3H]Pro2,4 substance P perfused through the lungs demonstrated that the major products were consistent with intact substance P, substance P 1–4, and smaller peptides; only minor amounts of products consistent with substance P 1–7, 1–9, or 3–11 were identified. These data support our previous findings showing that the physiological effects of intravascular substance P are limited by peptide degradation; the latter process, once begun, proceeds rapidly to nearly complete peptide degradation.
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Forte, Madonna, Schiavon, Valenti, Versaci, Zoccai, Frati, and Sciarretta. "Cardiovascular Pleiotropic Effects of Natriuretic Peptides." International Journal of Molecular Sciences 20, no. 16 (August 8, 2019): 3874. http://dx.doi.org/10.3390/ijms20163874.
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Atrial natriuretic peptide (ANP) is a cardiac hormone belonging to the family of natriuretic peptides (NPs). ANP exerts diuretic, natriuretic, and vasodilatory effects that contribute to maintain water–salt balance and regulate blood pressure. Besides these systemic properties, ANP displays important pleiotropic effects in the heart and in the vascular system that are independent of blood pressure regulation. These functions occur through autocrine and paracrine mechanisms. Previous works examining the cardiac phenotype of loss-of-function mouse models of ANP signaling showed that both mice with gene deletion of ANP or its receptor natriuretic peptide receptor A (NPR-A) developed cardiac hypertrophy and dysfunction in response to pressure overload and chronic ischemic remodeling. Conversely, ANP administration has been shown to improve cardiac function in response to remodeling and reduces ischemia-reperfusion (I/R) injury. ANP also acts as a pro-angiogenetic, anti-inflammatory, and anti-atherosclerotic factor in the vascular system. Pleiotropic effects regarding brain natriuretic peptide (BNP) and C-type natriuretic peptide (CNP) were also reported. In this review, we discuss the current evidence underlying the pleiotropic effects of NPs, underlying their importance in cardiovascular homeostasis.
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Ichimura, Keiichi, Hiroyuki Mineda, and Atsuro Seki. "Vascular Effects of Neuropeptides on Nasal Mucosa." Annals of Otology, Rhinology & Laryngology 97, no. 3 (May 1988): 289–93. http://dx.doi.org/10.1177/000348948809700316.
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We used dog nasal blood vessels and an in vitro muscle tension-detecting technique to examine the vascular effects of several neuropeptides: Vasoactive intestinal polypeptide, substance P, neurotensin, somatostatin, and neuropeptide Y (NPY). Electrically induced vasoconstriction was inhibited by every peptide except neurotensin, which enhanced this response. Every preparation treated with somatostatin, and one tissue treated with NPY, showed an enhanced noradrenaline-induced contraction. Only NPY caused a tissue contraction. Preparations precontracted by methoxamine were relaxed by every peptide. These results indicate that all peptides examined have marked but varied vasoactivities.
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Akagi, Keiko, Taku Nagao, and Tetsuro Urushidani. "Responsiveness of β-escin-permeabilized rabbit gastric gland model: effects of functional peptide fragments." American Journal of Physiology-Gastrointestinal and Liver Physiology 277, no. 3 (September 1, 1999): G736—G744. http://dx.doi.org/10.1152/ajpgi.1999.277.3.g736.
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We established a β-escin-permeabilized gland model with the use of rabbit isolated gastric glands. The glands retained an ability to secrete acid, monitored by [14C]aminopyrine accumulation, in response to cAMP, forskolin, and histamine. These responses were all inhibited by cAMP-dependent protein kinase inhibitory peptide. Myosin light-chain kinase inhibitory peptide also suppressed aminopyrine accumulation, whereas the inhibitory peptide of protein kinase C or that of calmodulin kinase II was without effect. Guanosine-5′- O-(3-thiotriphosphate) (GTPγS) abolished cAMP-stimulated acid secretion concomitantly, interfering with the redistribution of H+-K+-ATPase from tubulovesicles to the apical membrane. To identify the targets of GTPγS, effects of peptide fragments of certain GTP-binding proteins were examined. Although none of the peptides related to Rab proteins showed any effect, the inhibitory peptide of Arf protein inhibited cAMP-stimulated secretion. These results demonstrate that our new model, the β-escin-permeabilized gland, allows the introduction of relatively large molecules, e.g., peptides, into the cell, and will be quite useful for analyzing signal transduction of parietal cell function.
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Armas, Federica, Adriana Di Stasi, Mario Mardirossian, Antonello A. Romani, Monica Benincasa, and Marco Scocchi. "Effects of Lipidation on a Proline-Rich Antibacterial Peptide." International Journal of Molecular Sciences 22, no. 15 (July 26, 2021): 7959. http://dx.doi.org/10.3390/ijms22157959.
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The emergence of multidrug-resistant bacteria is a worldwide health problem. Antimicrobial peptides have been recognized as potential alternatives to conventional antibiotics, but still require optimization. The proline-rich antimicrobial peptide Bac7(1-16) is active against only a limited number of Gram-negative bacteria. It kills bacteria by inhibiting protein synthesis after its internalization, which is mainly supported by the bacterial transporter SbmA. In this study, we tested two different lipidated forms of Bac7(1-16) with the aim of extending its activity against those bacterial species that lack SbmA. We linked a C12-alkyl chain or an ultrashort cationic lipopeptide Lp-I to the C-terminus of Bac7(1-16). Both the lipidated Bac-C12 and Bac-Lp-I forms acquired activity at low micromolar MIC values against several Gram-positive and Gram-negative bacteria. Moreover, unlike Bac7(1-16), Bac-C12, and Bac-Lp-I did not select resistant mutants in E. coli after 14 times of exposure to sub-MIC concentrations of the respective peptide. We demonstrated that the extended spectrum of activity and absence of de novo resistance are likely related to the acquired capability of the peptides to permeabilize cell membranes. These results indicate that C-terminal lipidation of a short proline-rich peptide profoundly alters its function and mode of action and provides useful insights into the design of novel broad-spectrum antibacterial agents.
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Li, Yue, Zhenghua Tang, Paras N. Prasad, Marc R. Knecht, and Mark T. Swihart. "Peptide-mediated synthesis of gold nanoparticles: effects of peptide sequence and nature of binding on physicochemical properties." Nanoscale 6, no. 6 (2014): 3165–72. http://dx.doi.org/10.1039/c3nr06201e.
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Gargosky, S. E., J. C. Wallace, F. M. Upton, and F. J. Ballard. "C-terminal bombesin sequence requirements for binding and effects on protein synthesis in Swiss 3T3 cells." Biochemical Journal 247, no. 2 (October 15, 1987): 427–32. http://dx.doi.org/10.1042/bj2470427.
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1. Synthetic peptides corresponding to the five, seven, nine and eleven C-terminal amino acids of the tetradecapeptide bombesin as well as bombesin itself and gastrin-releasing peptide have been evaluated in Swiss 3T3 cells in order to define the minimal peptide length needed for biological responsiveness. 2. Gastrin-releasing peptide, bombesin, the undecapeptide and nonapeptide had nearly equipotent abilities to compete for binding of labelled gastrin-releasing peptide to the cell receptors and showed half-maximal competition at 5-10 nM. The heptapeptide and pentapeptide were ineffective. 3. Cross-linking experiments demonstrated specific binding of gastrin-releasing peptide to a 100 kDa receptor subunit. 4. Total cell protein synthesis was stimulated equally by the nonapeptide and longer peptides with a half-maximal effect at 0.5 nM, while a more than 1000-fold higher concentration of the heptapeptide was required to produce a similar response. Comparable results were found when insulin was also present. 5. Neither an inhibition of protein breakdown nor a stimulation of DNA labelling could be demonstrated by bombesin or gastrin-releasing peptide. 6. We conclude that a C-terminal peptide ligand comprising more than seven but no more than nine amino acids is required to achieve high-affinity binding and receptor-mediated responses via the bombesin receptor.
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Fernandes, Eduardo F. A., Linda M. Haugaard-Kedström, and Kristian Strømgaard. "The Effects of Lipidation on a TAT-Containing Peptide-Based Inhibitor of PSD-95." Australian Journal of Chemistry 73, no. 4 (2020): 307. http://dx.doi.org/10.1071/ch19392.
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Stability and cell permeability are critical parameters in the development of peptide therapeutics. Conjugation to fatty acids and cell-penetrating peptides, such as TAT (YGRKKRRQRRR), are established strategies to increase peptide stability and permeation, respectively. Here, we prepared lipidated analogues of a potent TAT-containing dimeric peptide-based inhibitor of the intracellular scaffolding protein PSD-95, an emerging drug target in ischaemic stroke. Lipidation increased peptide stability in vitro and in vivo. Combining both lipidation and conjugation to TAT improved brain/plasma ratios, but caused acute toxic effects due to the potent haemolytic activity of the TAT-lipid moiety.
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Shabab, Mohammed, Markus F. F. Arnold, Jon Penterman, Andrew J. Wommack, Hartmut T. Bocker, Paul A. Price, Joel S. Griffitts, Elizabeth M. Nolan, and Graham C. Walker. "Disulfide cross-linking influences symbiotic activities of nodule peptide NCR247." Proceedings of the National Academy of Sciences 113, no. 36 (August 22, 2016): 10157–62. http://dx.doi.org/10.1073/pnas.1610724113.
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Interactions of rhizobia with legumes establish the chronic intracellular infection that underlies symbiosis. Within nodules of inverted repeat-lacking clade (IRLC) legumes, rhizobia differentiate into nitrogen-fixing bacteroids. This terminal differentiation is driven by host nodule-specific cysteine-rich (NCR) peptides that orchestrate the adaptation of free-living bacteria into intracellular residents. Medicago truncatula encodes a family of >700 NCR peptides that have conserved cysteine motifs. NCR247 is a cationic peptide with four cysteines that can form two intramolecular disulfide bonds in the oxidized forms. This peptide affects Sinorhizobium meliloti transcription, translation, and cell division at low concentrations and is antimicrobial at higher concentrations. By preparing the three possible disulfide–cross-linked NCR247 regioisomers, the reduced peptide, and a variant lacking cysteines, we performed a systematic study of the effects of intramolecular disulfide cross-linking and cysteines on the activities of an NCR peptide. The relative activities of the five NCR247 variants differed strikingly among the various bioassays, suggesting that the NCR peptide-based language used by plants to control the development of their bacterial partners during symbiosis is even greater than previously recognized. These patterns indicate that certain NCR bioactivities require cysteines whereas others do not. The results also suggest that NCR247 may exert some of its effects within the cell envelope whereas other activities occur in the cytoplasm. BacA, a membrane protein that is critical for symbiosis, provides protection against all bactericidal forms of NCR247. Oxidative folding protects NCR247 from degradation by the symbiotically relevant metalloprotease HrrP (host range restriction peptidase), suggesting that disulfide bond formation may additionally stabilize NCR peptides during symbiosis.
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Cozza, Eduardo N., Mark F. Foecking, Maria del Carmen Vila, and Celso E. Gomez-Sanchez. "Adrenal receptors for natriuretic peptides and inhibition of aldosterone secretion in calf zona glomerulosa cells in culture." Acta Endocrinologica 129, no. 1 (July 1993): 59–64. http://dx.doi.org/10.1530/acta.0.1290059.
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Atrial and brain natriuretic peptides specifically bind to primary cultures of calf adrenal glomerulosa cells. Binding of both natriuretic peptides to the same receptor has been proved by: a Dixon plot showing competitive effects for the binding of 125I-labeled brain natriuretic peptide in the presence of increasing concentrations of unlabeled atrial natriuretic peptide; a Scatchard plot showing a lower dissociation constant (Kd) for atrial natriuretic peptide than for brain natriuretic peptide binding, but the maximum binding (Bmax) values were the same; autoradiography of sodium dodecyl sulfate polyacrylamide gels after cross-linking of 125I-labeled atrial natriuretic peptide and 125I-labeled brain natriuretic peptide, showing the same molecular weights for both peptide receptors—a single 66-kD band in whole cells and a main band at 125 kD in membranes. C-Type atrial natriuretic peptide only slightly displaced atrial natriuretic peptide binding. Angiotensin II- and potassium-mediated stimulation of aldosterone production were inhibited strongly and to the same degree by atrial and brain natriuretic peptide but only slightly by C-type atrial natriuretic peptide. Stimulation of aldosterone production mediated by adrenocorticotropin was only partially inhibited by atrial and brain natriuretic peptide, while baseline aldosterone was not affected. These results suggest that atrial and brain natriuretic peptide bind to the same receptors and provoke the same effects on aldosterone production. The weak effects found with C-type atrial natriuretic peptide suggest that the primary culture of calf adrenal glomerulosa cells contain the guanylate cyclase A receptor.
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Nordström, Randi, Lina Nyström, Humaira Ilyas, Hanudatta S. Atreya, Bruno C. Borro, Anirban Bhunia, and Martin Malmsten. "Microgels as carriers of antimicrobial peptides – Effects of peptide PEGylation." Colloids and Surfaces A: Physicochemical and Engineering Aspects 565 (March 2019): 8–15. http://dx.doi.org/10.1016/j.colsurfa.2018.12.049.
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MAGEE, COLM C., HARUHITO AZUMA, ANDREAS KNOFLACH, MARK D. DENTON, ANIL CHANDRAKER, SUHASINI IYER, ROLAND BUELOW, and MOHAMED SAYEGH. "In Vitro and in Vivo Immunomodulatory Effects of RDP1258, a Novel Synthetic Peptide." Journal of the American Society of Nephrology 10, no. 9 (September 1999): 1997–2005. http://dx.doi.org/10.1681/asn.v1091997.
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Abstract. Peptides derived from certain regions of human class I MHC molecules are known to have immunomodulatory effects. In particular, amino acid residues 75-84 of the HLA-B7 and HLA-B2702 molecules have demonstrated allele nonspecific immunosuppression in several animal transplant models. There is evidence that these effects are mediated by binding to intracellular heat shock proteins, including heme oxygenase-1. A new derivative of these peptides, RDP1258, was developed using a novel computer-assisted rational design technique. In vitro, RDP1258 peptide inhibited rat heme oxygenase activity in a dose-dependent manner. Similar to observations made with other in vitro heme oxygenase inhibitors, in vivo administration of RDP1258 peptide to naïve rats resulted in upregulation of splenic heme oxygenase activity. The effects of the peptide on alloimmune responses were then tested. Addition of RDP1258 to rat and human mixed leukocyte reactions inhibited proliferation in a dose-dependent manner. In a rat renal transplantation model, peptide therapy combined with a sub-therapeutic dose of cyclosporin A significantly prolonged allograft survival. These data provide further evidence that modulation of the heat shock protein heme oxygenase by rationally designed peptides affects immune effector functions and may allow the development of novel immunomodulatory strategies in organ transplantation.
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Solarte, Víctor A., Jaiver E. Rosas, Zuly J. Rivera, Martha L. Arango-Rodríguez, Javier E. García, and Jean-Paul Vernot. "A Tetrameric Peptide Derived from Bovine Lactoferricin Exhibits Specific Cytotoxic Effects against Oral Squamous-Cell Carcinoma Cell Lines." BioMed Research International 2015 (2015): 1–13. http://dx.doi.org/10.1155/2015/630179.
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Several short linear peptides derived from cyclic bovine lactoferricin were synthesized and tested for their cytotoxic effect against the oral cavity squamous-cell carcinoma (OSCC) cell lines CAL27 and SCC15. As a control, an immortalized and nontumorigenic cell line, Het-1A, was used. Linear peptides based on the RRWQWR core sequence showed a moderate cytotoxic effect and specificity towards tumorigenic cells. A tetrameric peptide, LfcinB(20–25)4, containing the RRWQWR motif, exhibited greater cytotoxic activity (>90%) in both OSCC cell lines compared to the linear lactoferricin peptide or the lactoferrin protein. Additionally, this tetrameric peptide showed the highest specificity towards tumorigenic cells among the tested peptides. Interestingly, this effect was very fast, with cell shrinkage, severe damage to cell membrane permeability, and lysis within one hour of treatment. Our results are consistent with a necrotic effect rather than an apoptotic one and suggest that this tetrameric peptide could be considered as a new candidate for the therapeutic treatment of OSCC.
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Richards, Jennifer P., Alan H. Stephenson, Mary L. Ellsworth, and Randy S. Sprague. "Synergistic effects of C-peptide and insulin on low O2-induced ATP release from human erythrocytes." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 305, no. 11 (December 1, 2013): R1331—R1336. http://dx.doi.org/10.1152/ajpregu.00341.2013.
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Erythrocytes participate in the matching of oxygen (O2) delivery with local need in skeletal muscle via the release of O2and the vasodilator, ATP. It was reported that a concentration of insulin found in humans with insulin resistance inhibits low O2-induced ATP release. However, in vivo, insulin is coreleased with connecting peptide (C-peptide) at equimolar concentrations, but because of the shorter insulin half-life, the peptides circulate at ratios of C-peptide to insulin ranging from 1:1 to 6:1. Here, we investigate the hypothesis that C-peptide and insulin work synergistically to maintain low O2-induced ATP release from human erythrocytes. Using a thin-film tonometer to alter O2tension, we determined that either C-peptide or insulin alone inhibits low O2-induced ATP release in a concentration-dependent manner; however, coadministration of the peptides at a 1:1 ratio does not ( n = 5; P < 0.05). Because this ratio of C-peptide to insulin is not present in vivo for extended periods, we also investigated the effect of additional physiological ratios on ATP release. In the presence of insulin concentrations that would be found in fasting humans (0.05 nM), C-peptide to insulin ratios of 4:1 and 6:1 did not adversely affect low O2-induced ATP release. However, at a concentration of insulin found in the peripheral circulation of humans under postprandial conditions (0.5 nM), a ratio of C-peptide to insulin of 6:1 inhibited low O2-induced ATP release ( n = 5). These findings demonstrate a heretofore unrecognized synergism between C-peptide and insulin that could have physiological importance in the regulation of perfusion distribution in skeletal muscle.
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Alcaide-Hidalgo, Juan María, Miguel Romero, Juan Duarte, and Eduardo López-Huertas. "Antihypertensive Effects of Virgin Olive Oil (Unfiltered) Low Molecular Weight Peptides with ACE Inhibitory Activity in Spontaneously Hypertensive Rats." Nutrients 12, no. 1 (January 20, 2020): 271. http://dx.doi.org/10.3390/nu12010271.
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The low molecular weight peptide composition of virgin olive oil (VOO) is mostly unknown. We hypothesised that unfiltered VOO could possess low molecular weight peptides with antihypertensive activity. We produced unfiltered VOO and obtained a water-soluble peptide extract from it. The peptides were separated by size-exclusion using fast protein liquid chromatography, and the low molecular weight fraction was analysed by nanoscale liquid chromatography-Orbitrap coupled with tandem mass spectrometry and de novo sequencing. We selected 23 peptide sequences containing between 6 and 9 amino acids and molecular masses ranging 698–1017 Da. Those peptides were chemically synthesised and their angiotensin-converting enzyme (ACE) inhibitory activity was studied in vitro. Seven peptides showed a strong activity, with half maximal inhibitory concentration (IC50) <10 µm. The antihypertensive effects of the four most active synthesised ACE inhibitor peptides were studied in spontaneously hypertensive rats (SHR). Acute oral administration of synthetic peptides RDGGYCC and CCGNAVPQ showed antihypertensive activity in SHR. We conclude that unfiltered VOO naturally contains low molecular weight peptides with specific ACE inhibitory activity and antihypertensive effects in SHR.
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RUISSEN, Anita L. A., Jasper GROENINK, Eva J. HELMERHORST, Els WALGREEN-WETERINGS, Wim van't HOF, Enno C. I. VEERMAN, and Arie V. NIEUW AMERONGEN. "Effects of histatin 5 and derived peptides on Candida albicans." Biochemical Journal 356, no. 2 (May 24, 2001): 361–68. http://dx.doi.org/10.1042/bj3560361.
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Three anti-microbial peptides were compared with respect to their killing activity against Candida albicans and their ability to disturb its cellular and internal membranes. Histatin 5 is an anti-fungal peptide occurring naturally in human saliva, while dhvar4 and dhvar5 are variants of its active domain, with increased anti-microbial activity. dhvar4has increased amphipathicity compared with histatin 5, whereas dhvar5has amphipathicity comparable with that of histatin 5. All three peptides caused depolarization of the cytoplasmic and/or mitochondrial membrane, indicating membranolytic activity. For the variant peptides both depolarization and killing occurred at a faster rate. With FITC-labelled peptides, no association with the cytoplasmic membrane was observed, contradicting the formation of permanent transmembrane multimeric peptide pores. Instead, the peptides were internalized and act on internal membranes, as demonstrated with mitochondrion- and vacuole-specific markers. In comparison with histatin 5, the variant peptides showed a more destructive effect on mitochondria. Entry of the peptides and subsequent killing were dependent on the metabolic state of the cells. Blocking of the mitochondrial activity led to complete protection against histatin 5 activity, whereas that of dhvar4 was hardly affected and that of dhvar5 was affected only intermediately.
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Hou, Shuyu, Zhigang Liu, Anne W. Young, Sheron L. Mark, Neville R. Kallenbach, and Dacheng Ren. "Effects of Trp- and Arg-Containing Antimicrobial-Peptide Structure on Inhibition of Escherichia coli Planktonic Growth and Biofilm Formation." Applied and Environmental Microbiology 76, no. 6 (January 22, 2010): 1967–74. http://dx.doi.org/10.1128/aem.02321-09.
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ABSTRACT Biofilms are sessile microbial communities that cause serious chronic infections with high morbidity and mortality. In order to develop more effective approaches for biofilm control, a series of linear cationic antimicrobial peptides (AMPs) with various arginine (Arg or R) and tryptophan (Trp or W) repeats [(RW) n -NH2, where n = 2, 3, or 4] were rigorously compared to correlate their structures with antimicrobial activities affecting the planktonic growth and biofilm formation of Escherichia coli. The chain length of AMPs appears to be important for inhibition of bacterial planktonic growth, since the hexameric and octameric peptides significantly inhibited E. coli growth, while tetrameric peptide did not cause noticeable inhibition. In addition, all AMPs except the tetrameric peptide significantly reduced E. coli biofilm surface coverage and the viability of biofilm cells, when added at inoculation. In addition to inhibition of biofilm formation, significant killing of biofilm cells was observed after a 3-hour treatment of preformed biofilms with hexameric peptide. Interestingly, treatment with the octameric peptide caused significant biofilm dispersion without apparent killing of biofilm cells that remained on the surface; e.g., the surface coverage was reduced by 91.5 ± 3.5% by 200 μM octameric peptide. The detached biofilm cells, however, were effectively killed by this peptide. Overall, these results suggest that hexameric and octameric peptides are potent inhibitors of both bacterial planktonic growth and biofilm formation, while the octameric peptide can also disperse existing biofilms and kill the detached cells. These results are helpful for designing novel biofilm inhibitors and developing more effective therapeutic methods.
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Mohri, Hiroshi, and Takao Ohkubo. "Effects of Hybrid Peptide Analogs to Receptor Recognition Domains on α- and γ-Chains of Human Fibrinogen on Fibrinogen Binding to Platelets." Thrombosis and Haemostasis 69, no. 05 (1993): 490–95. http://dx.doi.org/10.1055/s-0038-1651639.
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SummaryWe synthesized a series of hybrid peptides that correspond to the γ-chain dodecapeptide (400-411), variable numbers of glycine residues, and the RGDS peptide [Y-HHLGGAK-QAGDV(G) n RGDS] to investigate the relationship of these receptor recognition domains of fibrinogen to platelet membrane glycoprotein IIb/IIIa. The tetrapeptide RGDS, the GRGDSPA peptide and the dodecapeptide inhibited binding of fibrinogen to GPIIb/IIIa by 50% (IC50) at concentrations of 17 ± 1.6 μM, 15 ± 2.1 μM, and 87 ± 6.8 μM, respectively. The inhibitory effect of hybrid peptides increased as the number of glycine residues increased, plateauing with 9-11 glycine residues in hybrid peptide analogs, which had an IC50 of 0.68 ± 0.14 μM. These hybrid peptides completely inhibited the binding of fibrinogen to activated platelets when used in sufficient concentrations. The peptide Y-HHLGGAKQAGDV(G)9RGDS blocked ADP-induced aggregation in citrated platelet-rich plasma with IC50 of 3.5 ± 0.6 μM. When the peptide Y-HHLGGAK-QAGDV(G)9RGDS was labeled with 125I to quantify its binding to platelets, maximal binding was observed within 30 min. The binding sites of the hybrid peptide were 43,600 molecules/platelet (K d = 3.1 ± 0.5 × 10-7 M) to stimulated platelets and 12,500 molecules/platelet (K d = 1.4 ± 0.2 × 10-7 M) to nonstimulated platelets. The hybrid peptides had the same binding affinity to platelets as fibrinogen and inhibited platelet function. Moreover, anti-GPIIb/IIIa antibody inhibited the binding of the labeled hybrid peptide to stimulated platelets. These results indicate that in the native fibrinogen molecule the presence of both RGD sequence or γ-chain domain at optimal distances increased the binding affinity to GPIIb/IIIa. These domains may be the source of hybrid peptide, expanding a new class of platelet inhibitors that act at membrane receptors for adhesive proteins.
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Strandberg, Erik, Deniz Tiltak, Marco Ieronimo, Nathalie Kanithasen, Parvesh Wadhwani, and Anne S. Ulrich. "Influence of C-terminal amidation on the antimicrobial and hemolytic activities of cationic α-helical peptides." Pure and Applied Chemistry 79, no. 4 (January 1, 2007): 717–28. http://dx.doi.org/10.1351/pac200779040717.
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The effect of C-terminal amidation on the antimicrobial and hemolytic activities of antimicrobial peptides was studied using three cationic peptides which form amphiphilic α-helices when bound to membranes. The natural antimicrobial peptide PGLa, the designer-made antibiotic MSI-103, and the cell-penetrating "model amphipathic peptide" (MAP) are all amidated in their original forms, and their biological activities were compared with the same sequences carrying a free C-terminus. It was found that, in general, a free COOH-terminus reduces both the antimicrobial activity and the hemolytic side effects of the peptides. The only exception was observed for MSI-103, whose antimicrobial activity was not decreased in the acid form. Having shown that the therapeutic index (TI) of this novel peptide is significantly higher than for the other tested peptides, with high antibiotic activity and little undesired effects, we suggest that it could be a useful starting point for further development of new peptide antibiotics.
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Obasse, Idira, Mark Taylor, Nigel J. Fullwood, and David Allsop. "Development of proteolytically stable N-methylated peptide inhibitors of aggregation of the amylin peptide implicated in type 2 diabetes." Interface Focus 7, no. 6 (October 20, 2017): 20160127. http://dx.doi.org/10.1098/rsfs.2016.0127.
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Islet amyloid polypeptide, also known as amylin, is the main component of the amyloid deposits present in approximately 90% of people with type 2 diabetes mellitus (T2DM). In this disease, amylin aggregates into multimeric β-pleated sheet structures which cause damage to pancreatic islet β-cells. Inhibitors of early-stage amylin aggregation could therefore provide a disease-modifying treatment for T2DM. In this study, overlapping peptides were designed to target the ‘binding’ region (RLANFLVHSS, residues 11–20) of human amylin, and their effects on amyloid fibril formation were determined by thioflavin-T assay. The first generation peptides showed less than 50% inhibition of aggregation, but a second generation peptide (H 2 N-RGANFLVHGR-CONH 2 ) showed strong inhibitory effects on amylin aggregation, and this was confirmed by negative stain electron microscopy. Cytotoxicity studies revealed that this peptide protected human pancreatic 1.4E7 (ECACC 10070102) insulin-secreting cells from the toxic effects of human amylin. Unlike the retro-inverso version of this peptide, which stimulated aggregation, two N-methylated peptides (H 2 N-RGAmNFmLVmHGR-CONH 2 and H 2 N-RGANmFLmVHmR-CONH 2 ) gave very clear dose-dependent inhibition of fibril formation. These two peptides were also stable against a range of different proteolytic enzymes, and in human plasma. These N-methylated peptides could provide a novel treatment for slowing progression of T2DM.
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Nossner, E., J. E. Goldberg, C. Naftzger, S. C. Lyu, C. Clayberger, and A. M. Krensky. "HLA-derived peptides which inhibit T cell function bind to members of the heat-shock protein 70 family." Journal of Experimental Medicine 183, no. 2 (February 1, 1996): 339–48. http://dx.doi.org/10.1084/jem.183.2.339.
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Synthetic peptides corresponding to sequences of HLA class I molecules have inhibitory effects on T cell function. The peptides investigated in this study have sequences corresponding to the relatively conserved region of the alpha 1 helix of HLA class I molecules that overlaps the "public epitope" Bw4/Bw6. These HLA-derived peptides exhibit inhibitory effects on T lymphocytes and have beneficial effects on the survival of allogenic organ transplants in mice and rats. Peptides corresponding to the Bw4a epitope appear most potent as they inhibit the differentiation of T cell precursors into mature cytotoxic T lymphocytes (CTL) and target cell lysis by established CTL lines and clones. To elucidate the mechanism through which these peptides mediate their inhibitory effect on T lymphocytes, peptide binding proteins were isolated from T cell lysates. We show that the inhibitory Bw4a peptide binds two members of the heat-shock protein (HSP) 70 family, constitutively expressed HSC70 and heat-inducible HSP70. Peptide binding to HSC/HSP70 is sequence specific and follows the rules defined by the HSC70 binding motif. Most intriguing, however, is the strict correlation of peptide binding to HSC/HSP70 and the functional effects such that only inhibitory peptides bind to HSC70 and HSP70 whereas noninhibitory peptides do not bind. This correlation suggests that small molecular weight HLA-derived peptides may modulate T cell responses by directly interacting with HSPs. In contrast to numerous reports of HSP70 expression at the surface of antigen-presenting cells and some tumor cells, we find no evidence that HSC/HSP70 are expressed at the surface of the affected T cells. Therefore, we believe that the peptides' immunodulatory effects are not mediated through a signaling event initiated by interaction of peptide with surface HSP, but favor a model similar to the action of other immunomodulatory compounds, FK506 and cyclosporin A, with a role for HSC/HSP70 similar to that for immunophilins, FKBPs and CyP40.
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Kannan, Arvind, Navam Hettiarachchy, and Satya Narayan. "Colon and Breast Anti-cancer Effects of Peptide Hydrolysates Derived from Rice Bran." Open Bioactive Compounds Journal 2, no. 1 (April 16, 2009): 17–20. http://dx.doi.org/10.2174/1874847300902010017.
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Rice bran is an economical, under-utilized co-product of rough rice milling. The objective of this study was to produce rice-bran peptides and investigate for anti-cancer activity. Protein hydrolysates were prepared by treating heat stabilized defatted rice-bran with food grade Alcalase enzyme, followed by treatment with simulated gastric and intestinal juices to obtain resistant peptides. Resistant peptides were fractionated into >50, 10-50, 5-10, and <5 kDa sizes, freeze dried, and evaluated for inhibitory and cytotoxicity activities on human colon (HCT-116) and breast (HTB-26) cancer cell lines. The results showed that <5 kDa fraction of rice-bran is a potent anti-cancer agent. The cytotoxicity of the fraction to both cancer cell types was more pronounced after the treatment with 500 µg/mL. The IC50 of the peptide fraction was approximately 750 µg/mL. These results indicate that the <5 kDa peptide fraction separated from rice bran protein hydrolysate has a potent anti-tumor activity for colon cancer cells. The peptide fractions that demonstrate anti-cancer activities have the potential for use as functional food ingredients for health benefits.
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Wong, Philip Ching Yat, Jun Guo, and Aidong Zhang. "The renal and cardiovascular effects of natriuretic peptides." Advances in Physiology Education 41, no. 2 (June 1, 2017): 179–85. http://dx.doi.org/10.1152/advan.00177.2016.
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The landmark report by de Bold et al. in 1981 signified the heart as one of the endocrine organs involved in fluid and salt balance (de Bold AJ, Borenstein HB, Veress AT, Sonnenberg H. Life Sci 28: 89–94, 1981). Atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) are secreted from cardiomyocytes in response to cardiac stretch as in the case of heart failure, whereas C-type natriuretic peptide (CNP) is secreted from endothelial and renal cells in response to cytokines and endothelium-dependent agonists, such as acetylcholine. Binding ANP or BNP to natriuretic peptide receptor A induces cyclic guanylyl monophosphate as second messenger in the target cells to mediate the following: natriuresis; water diuresis; increasing glomerular filtration rate; decreasing systemic sympathetic activities; plasma volume; cardiac output and blood pressure; and curbing mitoses of heart fibroblasts and hypertrophy of cardiovascular muscle cells. ANP, BNP, and CNP are cleared from the bloodstream by natriuretic peptide receptor C and degraded by an ectoenzyme called neprilysin (NEP). The plasma levels of BNP are typically >100 pg/ml in patients with congestive heart failure. Sacubitril/valsartan is an angiotensin receptor NEP inhibitor that prevents the clinical progression of surviving patients with heart failure more effectively than enalapril, an angiotensin-converting enzyme inhibitor. A thorough understanding of the renal and cardiovascular effects of natriuretic peptides is of major importance for first-year medical students to gain insight into the significance of plasma levels of BNP in patients with heart failure.
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Kojima, Suzuka, Hitomi Nakamura, Sungho Lee, Fukue Nagata, and Katsuya Kato. "Hydroxyapatite Formation on Self-Assembling Peptides with Differing Secondary Structures and Their Selective Adsorption for Proteins." International Journal of Molecular Sciences 20, no. 18 (September 19, 2019): 4650. http://dx.doi.org/10.3390/ijms20184650.
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Self-assembling peptides have been employed as biotemplates for biomineralization, as the morphologies and sizes of the inorganic materials can be easily controlled. We synthesized two types of highly ordered self-assembling peptides with different secondary structures and investigated the effects of secondary structures on hydroxyapatite (HAp) biomineralization of peptide templates. All as-synthesized HAp-peptides have a selective protein adsorption capacity for basic protein (e.g., cytochrome c and lysozyme). Moreover, the selectivity was improved as peptide amounts increased. In particular, peptide–HAp templated on β-sheet peptides adsorbed more cytochrome c than peptide–HAp with α-helix structures, due to the greater than 2-times carboxyl group density at their surfaces. It can be expected that self-assembled peptide-templated HAp may be used as carriers for protein immobilization in biosensing and bioseparation applications and as enzyme-stabilizing agents.
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Rigel, D. F. "Effects of neuropeptides on heart rate in dogs: comparison of VIP, PHI, NPY, CGRP, and NT." American Journal of Physiology-Heart and Circulatory Physiology 255, no. 2 (August 1, 1988): H311—H317. http://dx.doi.org/10.1152/ajpheart.1988.255.2.h311.
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This study was designed to evaluate the potential chronotropic actions of several cardiac neuropeptides in pentobarbital-anesthetized dogs. After bilateral vagotomy and stellectomy and muscarinic receptor blockade, I injected vasoactive intestinal polypeptide, peptide histidine isoleucine, neuropeptide Y, neurotensin, and calcitonin gene-related peptide into the intact sinus node artery. Neurotensin, calcitonin gene-related peptide, and neuropeptide Y exhibited no physiologically significant changes in heart rate. However, the structural homologues vasoactive intestinal polypeptide and peptide histidine isoleucine each augmented heart rate with maximal increases (approximately 120 beats/min) similar to those of norepinephrine. Vasoactive intestinal polypeptide and peptide histidine isoleucine were twice and 1/18, respectively, as potent as norepinephrine. The cardioacceleratory responses to vasoactive intestinal polypeptide and peptide histidine isoleucine were more slowly developing and longer lasting than those of norepinephrine. The responses to these two peptides were unchanged after beta-adrenergic blockade with propranolol in a dose sufficient to eliminate or greatly attenuate the norepinephrine tachycardia. These results indicate a potential role of endogenous vasoactive intestinal polypeptide and peptide histidine isoleucine in nonadrenergic, noncholinergic heart rate control in the dog.
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Henning, R. "Vasoactive intestinal peptide: cardiovascular effects." Cardiovascular Research 49, no. 1 (January 2001): 27–37. http://dx.doi.org/10.1016/s0008-6363(00)00229-7.
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Patgiri, Anupam, Stephen T. Joy, and Paramjit S. Arora. "Nucleation Effects in Peptide Foldamers." Journal of the American Chemical Society 134, no. 28 (July 5, 2012): 11495–502. http://dx.doi.org/10.1021/ja301953j.
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Smolarczyk, Ryszard, Tomasz Cichoń, Wojciech Kamysz, Magdalena Głowala-Kosińska, Anna Szydło, Łukasz Szultka, Aleksander L. Sieroń, and Stanisław Szala. "Anticancer effects of CAMEL peptide." Laboratory Investigation 90, no. 6 (March 8, 2010): 940–52. http://dx.doi.org/10.1038/labinvest.2010.58.
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Wei, Wei, Shue Wang, Xue-Jun Zhang, Jiu-Xun Zhang, Zheng-Wang Chen, Jia-Ying Huang, and Ye-Wang Zhang. "The Effects of Mung Bean Peptide and Its’ Complexes on the Treatment of Lead Poisoning." Journal of Food Quality 2021 (July 22, 2021): 1–7. http://dx.doi.org/10.1155/2021/2851146.
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Objective. To investigate the effects of mung bean peptide and its’ complexes on promoting lead excretion and neuroprotection of zebrafish. Methods. The lead poisoning models of zebrafish were established by lead acetate solution; the models were treated with high and low concentrations (58.3 and 175 μg/mL) of mung bean peptides, with high, medium, and low concentrations (27.8, 83.3, and 250 μg/mL) of mung bean peptide complexes, separately. The effects of the mung bean peptide complexes on the lead content, axonal fluorescence intensity, and peripheral motor nerve length changes were identified in the zebrafish model, and the effects of mung bean peptide and its’ complexes on zebrafish's lead excretion, axonal protection rate, and peripheral movement promotion rate of nerve regeneration were calculated. Results. The effects of high concentration of mung bean peptide (175 μg/mL) in promoting lead excretion was 29% ( p < 0.05 ), and the effect of high concentration of mung bean peptide complexes (250 μg/mL) in promoting lead excretion was 30% ( p < 0.05 ). The other concentrations of mung bean peptide and its’ complex groups did not show a noticeable lead excretion effect. The protective effects of mung bean peptide at concentrations of 58.3 and 175 μg/mL against zebrafish axonal injury were 98% and 101% ( p < 0.01 ), and the peripheral nerve regeneration promotion effects were 29% ( p > 0.05 ) and 42% ( p < 0.05 ), respectively. The protective effects of mung bean peptide complexes at concentrations of 27.8, 83.3, and 250 μg/mL against zebrafish axonal injury were 85%, 78%, and 93% ( p < 0.01 ); peripheral nerve regeneration promotion rates were 46%, 50%, and 50% ( p < 0.05 ). Conclusion. The mung bean peptide and its’ complexes can effectively promote the discharge of lead in the zebrafish lead poisoning and have protective and regeneration effects on zebrafish nerves.
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Kellner, Michael, Ines Diehl, Kristina Knaudt, Cornelius Schüle, Holger Jahn, and Klaus Wiedemann. "C-type natriuretic peptide exerts stimulatory effects on the corticotropin-releasing hormone-induced secretion of hormones in normal man." European Journal of Endocrinology 136, no. 4 (April 1997): 388–93. http://dx.doi.org/10.1530/eje.0.1360388.
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Abstract C-type natriuretic peptide and atrial natriuretic peptide have been reported to bind to distinct receptors and to exert opposing effects on different systems. Although it is known that atrial natriuretic peptide inhibits the corticotropin-releasing hormone-stimulated hormone release in man, the corresponding action of C-type natriuretic peptide has so far not been characterized. We investigated the effects of 30-min infusions of 150 and 300 μg C-type natriuretic peptide on adrenocorticotropin, cortisol, and prolactin release stimulated by 100 μg corticotropin-releasing hormone and on cardiovascular parameters in 8 healthy male volunteers. Compared with placebo, 300 μg C-type natriuretic peptide significantly (P<0·05) enhanced the stimulation of cortisol (area under curve (arbitrary units): 520 ± 35 vs 651 ± 55) and prolactin (area under curve: 29 ± 3 vs 37 ± 5). Adrenocorticotropin levels were increased, but the differences did not reach statistical significance (maximum increment: 27±4 vs 36± 2 pg/ml). C-type natriuretic peptide at a dose of 150 μg had no clear effect on these hormones and C-type natriuretic peptide also produced no cardiovascular or subjective effects. Our data suggest stimulatory effects of C-type natriuretic peptide on corticotropinreleasing hormone-induced hormone release and offer further evidence for a complex role of different natriuretic peptides in endocrine regulation. European Journal of Endocrinology 136 388–393
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Kasetty, Gopinath, Praveen Papareddy, Martina Kalle, Victoria Rydengård, Matthias Mörgelin, Barbara Albiger, Martin Malmsten, and Artur Schmidtchen. "Structure-Activity Studies and Therapeutic Potential of Host Defense Peptides of Human Thrombin." Antimicrobial Agents and Chemotherapy 55, no. 6 (March 14, 2011): 2880–90. http://dx.doi.org/10.1128/aac.01515-10.
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ABSTRACTPeptides of the C-terminal region of human thrombin are released upon proteolysis and identified in human wounds. In this study, we wanted to investigate minimal determinants, as well as structural features, governing the antimicrobial and immunomodulating activity of this peptide region. Sequential amino acid deletions of the peptide GKYGFYTHVFRLKKWIQKVIDQFGE (GKY25), as well as substitutions at strategic and structurally relevant positions, were followed by analyses of antimicrobial activity against the Gram-negative bacteriaEscherichia coliandPseudomonas aeruginosa, the Gram-positive bacteriumStaphylococcus aureus, and the fungusCandida albicans. Furthermore, peptide effects on lipopolysaccharide (LPS)-, lipoteichoic acid-, or zymosan-induced macrophage activation were studied. The thrombin-derived peptides displayed length- and sequence-dependent antimicrobial as well as immunomodulating effects. A peptide length of at least 20 amino acids was required for effective anti-inflammatory effects in macrophage models, as well as optimal antimicrobial activity as judged by MIC assays. However, shorter (>12 amino acids) variants also displayed significant antimicrobial effects. A central K14 residue was important for optimal antimicrobial activity. Finally, one peptide variant, GKYGFYTHVFRLKKWIQKVI (GKY20) exhibiting improved selectivity, i.e., low toxicity and a preserved antimicrobial as well as anti-inflammatory effect, showed efficiency in mouse models of LPS shock andP. aeruginosasepsis. The work defines structure-activity relationships of C-terminal host defense peptides of thrombin and delineates a strategy for selecting peptide epitopes of therapeutic interest.
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Björstad, Åse, Huamei Fu, Anna Karlsson, Claes Dahlgren, and Johan Bylund. "Interleukin-8-Derived Peptide Has Antibacterial Activity." Antimicrobial Agents and Chemotherapy 49, no. 9 (September 2005): 3889–95. http://dx.doi.org/10.1128/aac.49.9.3889-3895.2005.
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ABSTRACT Chemokines are inflammatory mediators with effects on diverse processes associated with the immune response. Some of the proteins belonging to the CXC chemokine subfamily, one of four groups in the family, possess inherent antibacterial activity against a wide range of bacteria. The CXC chemokine interleukin-8 (IL-8) has not been ascribed any direct antibacterial activity, but the fact that several of the amino acids in the carboxy-terminal part of the protein are identical or similar to those in a bactericidal cecropin-like peptide [Hp(2-20)] from Helicobacter pylori suggests that processing of the cytokine might generate peptide fragments with antibacterial properties. Synthetic peptides representing the carboxy-terminal part of IL-8 were investigated for antibacterial activities. These fragments possessed an antibacterial activity absent in the full-length IL-8. The antibacterial effects were reduced at increasing salt concentrations whereas the activity was increased when the pH was lowered. The IL-8-derived peptide shared structural similarity with and was also functionally additive to the Hp(2-20) peptide. The IL-8-derived peptide lacked the proinflammatory effects of the full-length protein. We also showed that acid hydrolysis of IL-8 generated a major peptide fragment corresponding to the antibacterial carboxyl terminus of the protein. The results presented are of special interest when put in the context of the suggested importance of antimicrobial peptides for microbial colonization of the gastric mucosa.
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Abu-Hamdah, Rania, Atoosa Rabiee, Graydon S. Meneilly, Richard P. Shannon, Dana K. Andersen, and Dariush Elahi. "The Extrapancreatic Effects of Glucagon-Like Peptide-1 and Related Peptides." Journal of Clinical Endocrinology & Metabolism 94, no. 6 (June 1, 2009): 1843–52. http://dx.doi.org/10.1210/jc.2008-1296.
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Fleeman, Renee M., Luis A. Macias, Jennifer S. Brodbelt, and Bryan W. Davies. "Defining principles that influence antimicrobial peptide activity against capsulatedKlebsiella pneumoniae." Proceedings of the National Academy of Sciences 117, no. 44 (October 21, 2020): 27620–26. http://dx.doi.org/10.1073/pnas.2007036117.
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The extracellular polysaccharide capsule ofKlebsiella pneumoniaeresists penetration by antimicrobials and protects the bacteria from the innate immune system. Host antimicrobial peptides are inactivated by the capsule as it impedes their penetration to the bacterial membrane. While the capsule sequesters most peptides, a few antimicrobial peptides have been identified that retain activity against encapsulatedK. pneumoniae,suggesting that this bacterial defense can be overcome. However, it is unclear what factors allow peptides to avoid capsule inhibition. To address this, we created a peptide analog with strong antimicrobial activity toward severalK. pneumoniaestrains from a previously inactive peptide. We characterized the effects of these two peptides onK. pneumoniae, along with their physical interactions withK. pneumoniaecapsule. Both peptides disrupted bacterial cell membranes, but only the active peptide displayed this activity against capsulatedK. pneumoniae. Unexpectedly, the active peptide showed no decrease in capsule binding, but did lose secondary structure in a capsule-dependent fashion compared with the inactive parent peptide. We found that these characteristics are associated with capsule-peptide aggregation, leading to disruption of theK. pneumoniaecapsule. Our findings reveal a potential mechanism for disrupting the protective barrier thatK. pneumoniaeuses to avoid the immune system and last-resort antibiotics.
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Khavinson, Vladimir, Anastasiia Ilina, Nina Kraskovskaya, Natalia Linkova, Nina Kolchina, Ekaterina Mironova, Alexander Erofeev, and Michael Petukhov. "Neuroprotective Effects of Tripeptides—Epigenetic Regulators in Mouse Model of Alzheimer’s Disease." Pharmaceuticals 14, no. 6 (May 27, 2021): 515. http://dx.doi.org/10.3390/ph14060515.
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KED and EDR peptides prevent dendritic spines loss in amyloid synaptotoxicity in in vitro model of Alzheimer’s disease (AD). The objective of this paper was to study epigenetic mechanisms of EDR and KED peptides’ neuroprotective effects on neuroplasticity and dendritic spine morphology in an AD mouse model. Daily intraperitoneal administration of the KED peptide in 5xFAD mice from 2 to 4 months of age at a concentration of 400 μg/kg tended to increase neuroplasticity. KED and EDR peptides prevented dendritic spine loss in 5xFAD-M mice. Their action’s possible molecular mechanisms were investigated by molecular modeling and docking of peptides in dsDNA, containing all possible combinations of hexanucleotide sequences. Similar DNA sequences were found in the lowest-energy complexes of the studied peptides with DNA in the classical B-form. EDR peptide has binding sites in the promoter region of CASP3, NES, GAP43, APOE, SOD2, PPARA, PPARG, GDX1 genes. Protein products of these genes are involved in AD pathogenesis. The neuroprotective effect of EDR and KED peptides in AD can be defined by their ability to prevent dendritic spine elimination and neuroplasticity impairments at the molecular epigenetic level.
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Porcher, Christophe, Aurélie Juhem, André Peinnequin, Valérie Sinniger, and Bruno Bonaz. "Expression and effects of metabotropic CRF1 and CRF2 receptors in rat small intestine." American Journal of Physiology-Gastrointestinal and Liver Physiology 288, no. 5 (May 2005): G1091—G1103. http://dx.doi.org/10.1152/ajpgi.00302.2004.
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Corticotropin-releasing factor (CRF)-like peptides mediate their effects via two receptor subtypes, CRF1 and CRF2; these receptors have functional implication in the motility of the stomach and colon in rats. We evaluated expression and functions of CRF1 and CRF2 receptors in the rat small intestine (i.e., duodenum and ileum). CRF1–2-like immunoreactivity (CRF1–2-LI) was localized in fibers and neurons of the myenteric and submucosal ganglia. CRF1–2-LI was found in nerve fibers of the longitudinal and circular muscle layers, in the mucosa, and in mucosal cells. Quantitative RT-PCR showed a stronger expression of CRF2 than CRF1 in the ileum, whereas CRF1 expression was higher than CRF2 expression in the duodenum. Functional studies showed that CRF-like peptides increased duodenal phasic contractions and reduced ileal contractions. CRF1 antagonists (CP-154,526 and SSR125543Q) blocked CRF-like peptide-induced activation of duodenal motility but did not block CRF-like peptide-induced inhibition of ileal motility. In contrast, a CRF2 inhibitor (astressin2-B) blocked the effects of CRF-like peptides on ileal muscle contractions but did not influence CRF-like peptide-induced activation of duodenal motility. These results demonstrate the presence of CRF1–2 in the intestine and demonstrate that, in vitro, CRF-like peptides stimulate the contractile activity of the duodenum through CRF1 receptor while inhibiting phasic contractions of the ileum through CRF2 receptor. These results strongly suggest that CRF-like peptides play a major role in the regulatory mechanisms that underlie the neural control of small intestinal motility through CRF receptors.
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Rodrigues, Elaine G., Andrey S. Dobroff, Carlos P. Taborda, and Luiz R. Travassos. "Antifungal and antitumor models of bioactive protective peptides." Anais da Academia Brasileira de Ciências 81, no. 3 (September 2009): 503–20. http://dx.doi.org/10.1590/s0001-37652009000300015.
Full textAbstract:
Peptides are remarkably reactive molecules produced by a great variety of species and able to display a number of functions in uni-and multicellular organisms as mediators, agonists and regulating substances. Some of them exert cytotoxic effects on cells other than those that produced them, and may have a role in controlling subpopulations and protecting certain species or cell types. Presently, we focus on antifungal and antitumor peptides and discuss a few models in which specific sequences and structures exerted direct inhibitory effects or stimulated a protective immune response. The killer peptide, deduced from an antiidiotypic antibody, with several antimicrobial activities and other Ig-derived peptides with cytotoxic activities including antitumor effects, are models studied in vitro and in vivo. Peptide 10 from gp43 of P. brasiliensis (P10) and the vaccine perspective against paracoccidioidomycosis is another topic illustrating the protective effect in vivo against a pathogenic fungus. The cationic antimicrobial peptides with antitumor activities are mostly reviewed here. Local treatment of murine melanoma by the peptide gomesin is another model studied at the Experimental Oncology Unit of UNIFESP.
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Michalek, Matthias, Bruno Vincent, Rainer Podschun, Joachim Grötzinger, Burkhard Bechinger, and Sascha Jung. "Hydramacin-1 in Action: Scrutinizing the Barnacle Model." Antimicrobial Agents and Chemotherapy 57, no. 7 (April 15, 2013): 2955–66. http://dx.doi.org/10.1128/aac.02498-12.
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ABSTRACTHydramacin-1 (HM1) from the metazoanHydraexerts antimicrobial activity against a wide range of bacterial strains. Notably, HM1 induces the aggregation of bacterial cells, accompanied by precipitation. To date, the proposed mechanism of peptide-lipid interaction, termed the barnacle model, has not been described on the molecular level. Here, we show by biochemical and biophysical techniques that the lipid-peptide interactions of HM1 are initiated by electrostatic and hydrophobic effects, in particular, by tryptophan and neighboring polar amino acid residues that cause an interfacial localization of the peptide between two self-contained lipid bilayers. The high binding constants of HM1 upon lipid interaction are in the range of other potent antimicrobial peptides, e.g., magainin, and can be reasonably explained by two distinct epitopes on the surface of the peptide's global structure, which both contain SWT(K/R) motifs. The residues of this motif favor localization of the peptide in the head group region of phospholipid bilayers up to a penetration depth of 4 Å and a minor participation of the lipids' hydrocarbon regions. Our results expand the knowledge about the molecular modes of action antimicrobial peptides use to tackle their target cells. Furthermore, the aggregation of living bacteria by HM1 was observed for a broad range of Gram-positive and Gram-negative bacteria. Therefore, the detailed view of peptide-lipid interactions described by the barnacle model consolidates it among the established models.
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Al-Khafaji, Ali Jabbar Oleiwi. "The Effects of Extracted Peptide from Skin of Iraqi Frog (Rana ridibunda) on Human Leukemic Lymphocytes." Baghdad Science Journal 16, no. 1 (March 11, 2019): 0040. http://dx.doi.org/10.21123/bsj.16.1.0040.
Full textAbstract:
The purified frog skin peptides were tested on leukemic patients lymphocytes, which revealed effects of cytotoxicity. Four frogs (Rana ridibunda) were stimulated by single intra-peritoneal injection of norepinephrine-HCl . Five different peptides;1(18) A, 2(19) L, 3(20) I,4(21) E and 5(22) Y were isolated and quantified. The peptide 3(20)I had 5.87% of hemolysis, while healthy human lymphocytes cytotoxic activity was for 2(19)L with inhibition( -10.4%).All peptides were subjected to polyacrylamide gel electrophoresis. The results revealed peptides 1(18)A, 2(19)L, 3(20)I which appeared as low as 10 KDa marker. Theoretically, the whole polypeptide had a molecular weight 7488.61 Dalton and contained on 62.405 amino acid (a.a). The peptide 4(21)E had a highest inhibitory effect(46%) on tumor cell line L20B. Furthermore , peptides effects on acute and chronic myeloid lymphocytic leukemia patients cell cultures revealed peptides selectivity in their action according to their net charge and functional group as reactant proton donor by the evidence of peptide 5(22)Y, 16.22 Dalton so it was either N—terminus (--NH2) or C—terminus (--OH) that led to cross cell membrane then acted as antigen mediated and activated cells in a high significant value (-142.37± 47.69)for acute myeloid lymphocytic leukemia .Both of peptides 3(20) I and 2(19) L were revealed a highly significant differences within Chr.40 and Chr. 22 of inhibition effects by testing volumes 15 µl and 10 µl . Those inhibition effects were due to peptides reaction with mitochondrial membrane which led to apoptosis . Conclusion; Frog skin peptides have a therapeutically worth for malignant diseases. Also some of peptides were activated lymphocytes may to cure immunodeficiency.