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Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides

The rapid dissemination of antibiotic resistance accelerates the desire for new antibacterial agents. Here, a class of antimicrobial peptides (AMPs) is designed by modifying the structural parameters of a natural chickpea‐derived AMP–Leg2, termed “functionalized chickpea‐derived Leg2 antimicrobial p...

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Autores principales: He, Qiao, Yang, Zhehao, Zou, Zhipeng, Qian, Mengyan, Wang, Xiaolei, Zhang, Xinhui, Yin, Zhongping, Wang, Jinhai, Ye, Xingqian, Liu, Donghong, Guo, Mingming
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9951321/
https://www.ncbi.nlm.nih.gov/pubmed/36563134
http://dx.doi.org/10.1002/advs.202205301
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author He, Qiao
Yang, Zhehao
Zou, Zhipeng
Qian, Mengyan
Wang, Xiaolei
Zhang, Xinhui
Yin, Zhongping
Wang, Jinhai
Ye, Xingqian
Liu, Donghong
Guo, Mingming
author_facet He, Qiao
Yang, Zhehao
Zou, Zhipeng
Qian, Mengyan
Wang, Xiaolei
Zhang, Xinhui
Yin, Zhongping
Wang, Jinhai
Ye, Xingqian
Liu, Donghong
Guo, Mingming
author_sort He, Qiao
collection PubMed
description The rapid dissemination of antibiotic resistance accelerates the desire for new antibacterial agents. Here, a class of antimicrobial peptides (AMPs) is designed by modifying the structural parameters of a natural chickpea‐derived AMP–Leg2, termed “functionalized chickpea‐derived Leg2 antimicrobial peptides” (FCLAPs). Among the FCLAPs, KTA and KTR show superior antibacterial efficacy against the foodborne pathogen Escherichia coli (E. coli) O157:H7 (with MICs in the range of 2.5–4.7 µmol L(−1)) and demonstrate satisfactory feasibility in alleviating E. coli O157:H7‐induced intestinal infection. Additionally, the low cytotoxicity along with insusceptibility to antimicrobial resistance increases the potential of FCLAPs as appealing antimicrobials. Combining the multi‐omics profiling andpeptide‐membrane interaction assays, a unique dual‐targeting mode of action is characterized. To specify the antibacterial mechanism, microscopical observations, membrane‐related physicochemical properties studies, and mass spectrometry assays are further performed. Data indicate that KTA and KTR induce membrane damage by initially targeting the lipopolysaccharide (LPS), thus promoting the peptides to traverse the outer membrane. Subsequently, the peptides intercalate into the peptidoglycan (PGN) layer, blocking its synthesis, and causing a collapse of membrane structure. These findings altogether imply the great potential of KTA and KTR as promising antibacterial candidates in combating the growing threat of E. coli O157:H7.
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spelling pubmed-99513212023-02-25 Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides He, Qiao Yang, Zhehao Zou, Zhipeng Qian, Mengyan Wang, Xiaolei Zhang, Xinhui Yin, Zhongping Wang, Jinhai Ye, Xingqian Liu, Donghong Guo, Mingming Adv Sci (Weinh) Research Articles The rapid dissemination of antibiotic resistance accelerates the desire for new antibacterial agents. Here, a class of antimicrobial peptides (AMPs) is designed by modifying the structural parameters of a natural chickpea‐derived AMP–Leg2, termed “functionalized chickpea‐derived Leg2 antimicrobial peptides” (FCLAPs). Among the FCLAPs, KTA and KTR show superior antibacterial efficacy against the foodborne pathogen Escherichia coli (E. coli) O157:H7 (with MICs in the range of 2.5–4.7 µmol L(−1)) and demonstrate satisfactory feasibility in alleviating E. coli O157:H7‐induced intestinal infection. Additionally, the low cytotoxicity along with insusceptibility to antimicrobial resistance increases the potential of FCLAPs as appealing antimicrobials. Combining the multi‐omics profiling andpeptide‐membrane interaction assays, a unique dual‐targeting mode of action is characterized. To specify the antibacterial mechanism, microscopical observations, membrane‐related physicochemical properties studies, and mass spectrometry assays are further performed. Data indicate that KTA and KTR induce membrane damage by initially targeting the lipopolysaccharide (LPS), thus promoting the peptides to traverse the outer membrane. Subsequently, the peptides intercalate into the peptidoglycan (PGN) layer, blocking its synthesis, and causing a collapse of membrane structure. These findings altogether imply the great potential of KTA and KTR as promising antibacterial candidates in combating the growing threat of E. coli O157:H7. John Wiley and Sons Inc. 2022-12-23 /pmc/articles/PMC9951321/ /pubmed/36563134 http://dx.doi.org/10.1002/advs.202205301 Text en © 2022 The Authors. Advanced Science published by Wiley‐VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
He, Qiao
Yang, Zhehao
Zou, Zhipeng
Qian, Mengyan
Wang, Xiaolei
Zhang, Xinhui
Yin, Zhongping
Wang, Jinhai
Ye, Xingqian
Liu, Donghong
Guo, Mingming
Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides
title Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides
title_full Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides
title_fullStr Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides
title_full_unstemmed Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides
title_short Combating Escherichia coli O157:H7 with Functionalized Chickpea‐Derived Antimicrobial Peptides
title_sort combating escherichia coli o157:h7 with functionalized chickpea‐derived antimicrobial peptides
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9951321/
https://www.ncbi.nlm.nih.gov/pubmed/36563134
http://dx.doi.org/10.1002/advs.202205301
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