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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
Qin,Haixin1,2,3; Zuo,Weimin1,2,3; Ge,Lilin4; Siu,Shirley W.I.5; Wang,Lei6; Chen,Xiaoling6; Ma,Chengbang6; Chen,Tianbao6; Zhou,Mei6; Cao,Zhijian7; Kwok,Hang Fai1,2,3
2023-01
Source PublicationComputational and Structural Biotechnology Journal
ISSN2001-0370
Volume21Pages:2960-2972
Abstract

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.

KeywordAnticancer Peptide Antimicrobial Peptide Brevinin Peptide Molecular Dynamic Simulation Peptide Modification
DOI10.1016/j.csbj.2023.05.006
URLView the original
Indexed BySCIE
Language英語English
WOS Research AreaBiochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS SubjectBiochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS IDWOS:001002496600001
PublisherElsevier B.V.
Scopus ID2-s2.0-85159150953
Fulltext Access
Citation statistics
Document TypeJournal article
CollectionFaculty of Health Sciences
DEPARTMENT OF BIOMEDICAL SCIENCES
Corresponding AuthorZhou,Mei
Affiliation1.Institute of Translational Medicine,Faculty of Health Sciences,University of Macau,Avenida da Universidade,Taipa,Macao
2.Department of Biomedical Sciences,Faculty of Health Sciences,University of Macau,Avenida da Universidade,Taipa,Macao
3.MoE Frontiers Science Center for Precision Oncology,University of Macau,Avenida da Universidade,Taipa,Macao
4.College of Pharmacy,Nanjing University of Chinese Medicine,Nanjing,210023,China
5.Institute of Science and Environment,University of Saint Joseph,Estrada Marginal da Ilha Verde,Macao
6.School of Pharmacy,Queen's University Belfast,Belfast,97 Lisburn Road,BT9 7BL,United Kingdom
7.State Key Laboratory of Virology and Modern Virology Research Center,College of Life Sciences,Wuhan University,Wuhan,430072,China
First Author AffilicationFaculty of Health Sciences;  University of Macau
Recommended Citation
GB/T 7714
Qin,Haixin,Zuo,Weimin,Ge,Lilin,et al. 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[J]. Computational and Structural Biotechnology Journal, 2023, 21, 2960-2972.
APA 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 (2023). 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. Computational and Structural Biotechnology Journal, 21, 2960-2972.
MLA Qin,Haixin,et al."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".Computational and Structural Biotechnology Journal 21(2023):2960-2972.
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