Antimicrobial Activity of the Antibacterial Peptide PMAP-GI24 and Its Analogs

Liu, Yongqing; Yan, Zhiling; Chai, Jun Meng; Zhou, Jiangfei; Wang, Chen

doi:10.1007/s10989-020-10026-6

Cited by 3 publications

(2 citation statements)

References 40 publications

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“…Wang et al pointed out that the cations of AMPs are important parameters that affect the antimicrobial activity of AMPs [ 25 ]. The positive charges of AMPs can interact electrostatically with the negatively charged components on the surface of microbial cells, resulting in disturbance of cell membrane permeability and cell death [ 26 ]. The presence of lysine (K), R and histidine (H) is the reason why AMPs are positively charged.…”

Section: Resultsmentioning

confidence: 99%

Design and heterologous expression of a novel dimeric LL37 variant in Pichia pastoris

et al. 2021

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Background The antimicrobial peptide LL37 is produced by white blood cells (mainly neutrophils) and various epithelial cells, and has the outstanding advantages of participating in immune regulation, causing chemotaxis of immune cells and promoting wound healing. However, the central domain of LL37 needs to be improved in terms of antimicrobial activity. Results In this study, the amino acid substitution method was used to improve the antimicrobial activity of the LL37 active center, and a dimeric design with a better selection index was selected. A flexible linker was selected and combined with the 6 × His-SUMO tag and LG was successfully expressed using Pichia pastoris as a host. Recombinant LG displayed strong antimicrobial activity by destroying the cell membrane of bacteria but had low hemolytic activity. In addition, compared with monomeric peptide FR, rLG had improved ability to tolerate salt ions. Conclusion This research provides new ideas for the production of modified AMPs in microbial systems and their application in industrial production.

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Section: Resultsmentioning

confidence: 99%

Design and heterologous expression of a novel dimeric LL37 variant in Pichia pastoris

et al. 2021

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“…In recent years, our group has performed research on the structural modification and antimicrobial activity of PMAPs. According to the structure and mechanism of PMAPs, many scholars have designed multiple novel modified peptides with increased stability and antimicrobial activity (43)(44)(45)(46)(47)(48)(49)(50). This review mainly summarizes the research progress on the structural characteristics and biological activities of PMAPs in recent years.…”

Section: Antimicrobial Peptidesmentioning

confidence: 99%

Porcine Myeloid Antimicrobial Peptides: A Review of the Activity and Latest Advances

et al. 2021

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Traditional antibiotics have made great contributions to human health and animal husbandry since the discovery of penicillin in 1928, but bacterial resistance and drug residues are growing threats to global public health due to the long-term uncontrolled application of antibiotics. There is a critical need to develop new antimicrobial drugs to replace antibiotics. Antimicrobial peptides (AMPs) are distributed in all kingdoms of life, presenting activity against pathogens as well as anticancer, anti-inflammatory, and immunomodulatory activities; consequently, they have prospects as new potential alternatives to antibiotics. Porcine myeloid antimicrobial peptides (PMAPs), the porcine cathelicidin family of AMPs, have been reported in the literature in recent years. PMAPs have become an important research topic due to their strong antibacterial activity. This review focuses on the universal trends in the biochemical parameters, structural characteristics and biological activities of PMAPs.

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Efficacy of Natural Antimicrobial Peptides Versus Peptidomimetic Analogues: A Systematic Review

et al. 2022

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Aims: This systematic review was carried out to determine whether synthetic peptidomimetics exhibit significant advantages over antimicrobial peptides (AMPs) in terms of in vitro potency. Structural features – molecular weight, charge and length – were examined for correlations with activity. Methods: Original research articles reporting minimum inhibitory concentration (MIC) values against Escherichia coli, indexed until 31 December 2020, were searched in PubMed/ScienceDirect/Google Scholar and evaluated using mixed-effects models. Results: In vitro antimicrobial activity of peptidomimetics resembled that of AMPs. Net charge significantly affected MIC values (p < 0.001) with a trend of 4.6% decrease for increments in charge by +1. Conclusion: AMPs and antibacterial peptidomimetics exhibit similar potencies, providing an opportunity to exploit the advantageous stability and bioavailability typically associated with peptidomimetics.

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Antimicrobial Activity of the Antibacterial Peptide PMAP-GI24 and Its Analogs

Cited by 3 publications

References 40 publications

Design and heterologous expression of a novel dimeric LL37 variant in Pichia pastoris

Design and heterologous expression of a novel dimeric LL37 variant in Pichia pastoris

Porcine Myeloid Antimicrobial Peptides: A Review of the Activity and Latest Advances

Efficacy of Natural Antimicrobial Peptides Versus Peptidomimetic Analogues: A Systematic Review

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