Highly potent antimicrobial peptide derivatives of bovine cateslytin

Postma, Tobias M.; Liskamp, Rob M. J.

doi:10.1039/c6ra17944d

Cited by 5 publications

(4 citation statements)

References 37 publications

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“…These factors were positively correlated with the anti-Salmonella activity, yielding enhanced potency. This finding is similar to observations with other amphipathic α-helical cationic AMPs, revealing that C-terminal amidation results in a greater positive charge, hydrophobicity, α-helicity, and antibacterial activity [44,45]. It displayed higher hydrophobicity and exerted more potency than its D-enantiomer variant (dKn2-5R-NH 2 ).…”

Section: All Kn2 Variants Exhibited Increased Anti-salmonella Through Bactericidal Activitysupporting

confidence: 87%

Antimicrobial Peptide Modifications against Clinically Isolated Antibiotic-Resistant Salmonella

et al. 2021

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Antimicrobial peptides are promising molecules to address the global antibiotic resistance problem, however, optimization to achieve favorable potency and safety is required. Here, a peptide-template modification approach was employed to design physicochemical variants based on net charge, hydrophobicity, enantiomer, and terminal group. All variants of the scorpion venom peptide BmKn-2 with amphipathic α-helical cationic structure exhibited an increased antibacterial potency when evaluated against multidrug-resistant Salmonella isolates at a MIC range of 4–8 µM. They revealed antibiofilm activity in a dose-dependent manner. Sheep red blood cells were used to evaluate hemolytic and cell selectivity properties. Peptide Kn2-5R-NH2, dKn2-5R-NH2, and 2F-Kn2-5R-NH2 (variants with +6 charges carrying amidated C-terminus) showed stronger antibacterial activity than Kn2-5R (a variant with +5 charges bearing free-carboxyl group at C-terminus). Peptide dKn2-5R-NH2 (d-enantiomer) exhibited slightly weaker antibacterial activity with much less hemolytic activity (higher hemolytic concentration 50) than Kn2-5R-NH2 (l-enantiomer). Furthermore, peptide Kn2-5R with the least hydrophobicity had the lowest hemolytic activity and showed the highest specificity to Salmonella (the highest selectivity index). This study also explained the relationship of peptide physicochemical properties and bioactivities that would fulfill and accelerate progress in peptide antibiotic research and development.

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Section: All Kn2 Variants Exhibited Increased Anti-salmonella Through Bactericidal Activitysupporting

confidence: 87%

Antimicrobial Peptide Modifications against Clinically Isolated Antibiotic-Resistant Salmonella

et al. 2021

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“…1. The mutations were strategically placed to increase the positive charge and hydrophobic moment to enhance the peptides' affinity for anionic membranes, 15,[43][44][45] without modifying the original structure as the amphipathic helix conformation is central for the antimicrobial activity. 46 For the KS-Cnd mutant, Ser11 and Ser22 were replaced by two lysines; for KH-Cnd, histidines 4, 15, and 17 were all replaced by lysines, and for KSH-Cnd, histidines and serines were all replaced by lysines.…”

Section: Chionodracine Analogs Designmentioning

confidence: 99%

Design and characterization of chionodracine-derived antimicrobial peptides with enhanced activity against drug-resistant human pathogens

et al. 2018

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“…Highly potent antimicrobial peptide derivatives of bovine cateslytin were described in a study by T. M. Postma and R. M. J. Liskamp [143]. Here, the authors described that the bovine cateslytin (RSMRLSFRARGYGFR) was significantly more potent than the human analog (SSMKLSFRARGYGF), as it contains two additional positively charged arginine residues.…”

Section: Introduction Of Protective Groups Non-natural Amino Acids and Cyclization: Combination Of Derivatizations And Hybrid Peptidesmentioning

confidence: 97%

Discovery, Optimization, and Clinical Application of Natural Antimicrobial Peptides

et al. 2021

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Antimicrobial peptides (AMPs) are widespread in multicellular organisms. These structurally diverse molecules are produced as the first line of defense against pathogens such as bacteria, viruses, fungi, and parasites. Also known as host defense peptides in higher eukaryotic organisms, AMPs display immunomodulatory and anticancer activities. During the last 30 years, technological advances have boosted the research on antimicrobial peptides, which have also attracted great interest as an alternative to tackling the antimicrobial resistance scenario mainly provoked by some bacterial and fungal pathogens. However, the introduction of natural AMPs in clinical trials faces challenges such as proteolytic digestion, short half-lives, and cytotoxicity upon systemic and oral application. Therefore, some strategies have been implemented to improve the properties of AMPs aiming to be used as effective therapeutic agents. In the present review, we summarize the discovery path of AMPs, focusing on preclinical development, recent advances in chemical optimization and peptide delivery systems, and their introduction into the market.

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Highly potent antimicrobial peptide derivatives of bovine cateslytin

Cited by 5 publications

References 37 publications

Antimicrobial Peptide Modifications against Clinically Isolated Antibiotic-Resistant Salmonella

Antimicrobial Peptide Modifications against Clinically Isolated Antibiotic-Resistant Salmonella

Design and characterization of chionodracine-derived antimicrobial peptides with enhanced activity against drug-resistant human pathogens

Discovery, Optimization, and Clinical Application of Natural Antimicrobial Peptides

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