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Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue

In the development and study of antimicrobial peptides (AMPs), researchers have kept a watchful eye on peptides from the brevinin family because of their extensive antimicrobial activities and anticancer potency. In this study, a novel brevinin peptide was isolated from the skin secretions of the Wu...

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Autores principales: Qin, Haixin, Zuo, Weimin, Ge, Lilin, Siu, Shirley W.I., Wang, Lei, Chen, Xiaoling, Ma, Chengbang, Chen, Tianbao, Zhou, Mei, Cao, Zhijian, Kwok, Hang Fai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10205438/
https://www.ncbi.nlm.nih.gov/pubmed/37228702
http://dx.doi.org/10.1016/j.csbj.2023.05.006
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author Qin, Haixin
Zuo, Weimin
Ge, Lilin
Siu, Shirley W.I.
Wang, Lei
Chen, Xiaoling
Ma, Chengbang
Chen, Tianbao
Zhou, Mei
Cao, Zhijian
Kwok, Hang Fai
author_facet Qin, Haixin
Zuo, Weimin
Ge, Lilin
Siu, Shirley W.I.
Wang, Lei
Chen, Xiaoling
Ma, Chengbang
Chen, Tianbao
Zhou, Mei
Cao, Zhijian
Kwok, Hang Fai
author_sort Qin, Haixin
collection PubMed
description In the development and study of antimicrobial peptides (AMPs), researchers have kept a watchful eye on peptides from the brevinin family because of their extensive antimicrobial activities and anticancer potency. In this study, a novel brevinin peptide was isolated from the skin secretions of the Wuyi torrent frog, Amolops wuyiensis (A. wuyiensisi), named B1AW (FLPLLAGLAANFLPQIICKIARKC). B1AW displayed anti-bacterial activity against Gram-positive bacteria Staphylococcus aureus (S. aureus), methicillin-resistant Staphylococcus aureus (MRSA), and Enterococcus faecalis (E. faecalis). B1AW-K was designed to broaden the antimicrobial spectrum of B1AW. The introduction of a lysine residue generated an AMP with enhanced broad-spectrum antibacterial activity. It also displayed the ability to inhibit the growth of human prostatic cancer PC-3, non-small lung cancer H838, and glioblastoma cancer U251MG cell lines. In molecular dynamic (MD) simulations, B1AW-K had a faster approach and adsorption to the anionic membrane than B1AW. Therefore, B1AW-K was considered a drug prototype with a dual effect, which deserves further clinical investigation and validation.
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spelling pubmed-102054382023-05-24 Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue Qin, Haixin Zuo, Weimin Ge, Lilin Siu, Shirley W.I. Wang, Lei Chen, Xiaoling Ma, Chengbang Chen, Tianbao Zhou, Mei Cao, Zhijian Kwok, Hang Fai Comput Struct Biotechnol J Research Article In the development and study of antimicrobial peptides (AMPs), researchers have kept a watchful eye on peptides from the brevinin family because of their extensive antimicrobial activities and anticancer potency. In this study, a novel brevinin peptide was isolated from the skin secretions of the Wuyi torrent frog, Amolops wuyiensis (A. wuyiensisi), named B1AW (FLPLLAGLAANFLPQIICKIARKC). B1AW displayed anti-bacterial activity against Gram-positive bacteria Staphylococcus aureus (S. aureus), methicillin-resistant Staphylococcus aureus (MRSA), and Enterococcus faecalis (E. faecalis). B1AW-K was designed to broaden the antimicrobial spectrum of B1AW. The introduction of a lysine residue generated an AMP with enhanced broad-spectrum antibacterial activity. It also displayed the ability to inhibit the growth of human prostatic cancer PC-3, non-small lung cancer H838, and glioblastoma cancer U251MG cell lines. In molecular dynamic (MD) simulations, B1AW-K had a faster approach and adsorption to the anionic membrane than B1AW. Therefore, B1AW-K was considered a drug prototype with a dual effect, which deserves further clinical investigation and validation. Research Network of Computational and Structural Biotechnology 2023-05-06 /pmc/articles/PMC10205438/ /pubmed/37228702 http://dx.doi.org/10.1016/j.csbj.2023.05.006 Text en © 2023 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Qin, Haixin
Zuo, Weimin
Ge, Lilin
Siu, Shirley W.I.
Wang, Lei
Chen, Xiaoling
Ma, Chengbang
Chen, Tianbao
Zhou, Mei
Cao, Zhijian
Kwok, Hang Fai
Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue
title Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue
title_full Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue
title_fullStr Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue
title_full_unstemmed Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue
title_short Discovery and analysis of a novel antimicrobial peptide B1AW from the skin secretion of Amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue
title_sort discovery and analysis of a novel antimicrobial peptide b1aw from the skin secretion of amolops wuyiensis and improving the membrane-binding affinity through the construction of the lysine-introduced analogue
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10205438/
https://www.ncbi.nlm.nih.gov/pubmed/37228702
http://dx.doi.org/10.1016/j.csbj.2023.05.006
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