The introduction of l -phenylalanine into antimicrobial peptide protonectin enhances the selective antibacterial activit
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ORIGINAL ARTICLE
The introduction of l‑phenylalanine into antimicrobial peptide protonectin enhances the selective antibacterial activity of its derivative phe‑Prt against Gram‑positive bacteria Jinxiu Peng1 · Shuai Qiu1 · Fengjing Jia1 · Lishi Zhang1 · Yuhang He1 · Fangfang Zhang2 · Mengmeng Sun1 · Yabo Deng1 · Yifei Guo1 · Zhaoqing Xu1 · Xiaolei Liang2 · Wenjin Yan1 · Kairong Wang1 Received: 5 August 2020 / Accepted: 13 November 2020 © Springer-Verlag GmbH Austria, part of Springer Nature 2020
Abstract Protonectin was a typical amphiphilic antimicrobial peptide with potent antimicrobial activity against Gram-positive and Gram-negative bacteria. In the present study, when its eleventh amino acid in the sequence was substituted by phenylalanine, the analog named phe-Prt showed potent antimicrobial activity against Gram-positive bacteria, but no antimicrobial activity against Gram-negative bacteria, indicating a significant selectivity between Gram-positive bacteria and Gram-negative bacteria. However, when Gram-negative bacteria were incubated with EDTA, the bacteria were susceptible to phe-Prt. Next, the binding effect of phe-Prt with LPS was determined. Our result showed that LPS could hamper the bactericidal activity of phe-Prt against Gram-positive bacteria. The result of zeta potential assay further confirmed the binding effect of phe-Prt with LPS for it could neutralize the surface charge of E. coli and LPS. Then, the effect of phe-Prt on the integrity of outer membrane of Gram-negative bacteria was determined. Our results showed that phe-Prt had a much weaker disturbance to the outer membrane of Gram-negative bacteria than the parent peptide protonectin. In summary, the introduction of l-phenylalanine into the sequence of antimicrobial peptide protonectin made phe-Prt show significant selectivity against Gram-positive bacteria, which could partly be attributed to the delay effect of LPS for phe-Prt to access to cell membrane. Although further study is still needed to clarify the exact mechanism of selectivity, the present study provided a strategy to develop antimicrobial peptides with selectivity toward Gram-positive and Gram-negative bacteria. Keywords Antimicrobial peptide phe-Prt · Gram-negative bacteria · Selectivity · LPS
Introduction
Handling editor: F. Albericio. * Wenjin Yan [email protected] * Kairong Wang [email protected] 1
Key laboratory of Preclinical Study for New Drugs of Gansu Province, Institute of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Research Unit of Peptide Science of Chinese Academy of Medical Sciences 2019RU066, Lanzhou University, Lanzhou, People’s Republic of China
Key Laboratory for Gynecologic Oncology of Gansu Province, Department of Gynecology, The First Hospital of Lanzhou University, Lanzhou University, Lanzhou, People’s Republic of China
2
The increasing emergence of multi-drug-resistant pathogenic microorganism in the past two decades causes a serious challenge to public health and medicine (Perez-Rodriguez and Taban 2019; Aira e
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