Cargando…

Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri

Antimicrobial peptides (AMPs) are considered potential alternatives to antibiotics due to their advantages in solving antibiotic resistance. Brevinin-2GUb, which was extracted from the skin secretion of Hylarana guentheri, is a peptide with modest antimicrobial activity. Several analogues were desig...

Descripción completa

Detalles Bibliográficos
Autores principales: Lin, Yaxian, Liu, Siyan, Xi, Xinping, Ma, Chengbang, Wang, Lei, Chen, Xiaoling, Shi, Zhanzhong, Chen, Tianbao, Shaw, Chris, Zhou, Mei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8388802/
https://www.ncbi.nlm.nih.gov/pubmed/34438945
http://dx.doi.org/10.3390/antibiotics10080895
_version_ 1783742720336986112
author Lin, Yaxian
Liu, Siyan
Xi, Xinping
Ma, Chengbang
Wang, Lei
Chen, Xiaoling
Shi, Zhanzhong
Chen, Tianbao
Shaw, Chris
Zhou, Mei
author_facet Lin, Yaxian
Liu, Siyan
Xi, Xinping
Ma, Chengbang
Wang, Lei
Chen, Xiaoling
Shi, Zhanzhong
Chen, Tianbao
Shaw, Chris
Zhou, Mei
author_sort Lin, Yaxian
collection PubMed
description Antimicrobial peptides (AMPs) are considered potential alternatives to antibiotics due to their advantages in solving antibiotic resistance. Brevinin-2GUb, which was extracted from the skin secretion of Hylarana guentheri, is a peptide with modest antimicrobial activity. Several analogues were designed to explore the structure–activity relationship and enhance its activity. In general, the Rana box is not an indispensable motif for the bioactivity of Brevinin-2GUb, and the first to the 19th amino acids at the N-terminal end are active fragments, such that shortening the peptide while maintaining its bioactivity is a promising strategy for the optimisation of peptides. Keeping a complete hydrophobic face and increasing the net charges are key factors for antimicrobial activity. With the increase of cationic charges, α-helical proportion, and amphipathicity, the activity of t-Brevinin-2GUb-6K (tB2U-6K), in combatting bacteria, drastically improved, especially against Gram-negative bacteria, and the peptide attained the capacity to kill clinical isolates and fungi as well, which made it possible to address some aspects of antibiotic resistance. Thus, peptide tB2U-6K, with potent antimicrobial activity against antibiotic-resistant bacteria, the capacity to inhibit the growth of biofilm, and low toxicity against normal cells, is of value to be further developed into an antimicrobial agent.
format Online
Article
Text
id pubmed-8388802
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-83888022021-08-27 Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri Lin, Yaxian Liu, Siyan Xi, Xinping Ma, Chengbang Wang, Lei Chen, Xiaoling Shi, Zhanzhong Chen, Tianbao Shaw, Chris Zhou, Mei Antibiotics (Basel) Article Antimicrobial peptides (AMPs) are considered potential alternatives to antibiotics due to their advantages in solving antibiotic resistance. Brevinin-2GUb, which was extracted from the skin secretion of Hylarana guentheri, is a peptide with modest antimicrobial activity. Several analogues were designed to explore the structure–activity relationship and enhance its activity. In general, the Rana box is not an indispensable motif for the bioactivity of Brevinin-2GUb, and the first to the 19th amino acids at the N-terminal end are active fragments, such that shortening the peptide while maintaining its bioactivity is a promising strategy for the optimisation of peptides. Keeping a complete hydrophobic face and increasing the net charges are key factors for antimicrobial activity. With the increase of cationic charges, α-helical proportion, and amphipathicity, the activity of t-Brevinin-2GUb-6K (tB2U-6K), in combatting bacteria, drastically improved, especially against Gram-negative bacteria, and the peptide attained the capacity to kill clinical isolates and fungi as well, which made it possible to address some aspects of antibiotic resistance. Thus, peptide tB2U-6K, with potent antimicrobial activity against antibiotic-resistant bacteria, the capacity to inhibit the growth of biofilm, and low toxicity against normal cells, is of value to be further developed into an antimicrobial agent. MDPI 2021-07-22 /pmc/articles/PMC8388802/ /pubmed/34438945 http://dx.doi.org/10.3390/antibiotics10080895 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Lin, Yaxian
Liu, Siyan
Xi, Xinping
Ma, Chengbang
Wang, Lei
Chen, Xiaoling
Shi, Zhanzhong
Chen, Tianbao
Shaw, Chris
Zhou, Mei
Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri
title Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri
title_full Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri
title_fullStr Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri
title_full_unstemmed Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri
title_short Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri
title_sort study on the structure-activity relationship of an antimicrobial peptide, brevinin-2gub, from the skin secretion of hylarana guentheri
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8388802/
https://www.ncbi.nlm.nih.gov/pubmed/34438945
http://dx.doi.org/10.3390/antibiotics10080895
work_keys_str_mv AT linyaxian studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri
AT liusiyan studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri
AT xixinping studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri
AT machengbang studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri
AT wanglei studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri
AT chenxiaoling studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri
AT shizhanzhong studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri
AT chentianbao studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri
AT shawchris studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri
AT zhoumei studyonthestructureactivityrelationshipofanantimicrobialpeptidebrevinin2gubfromtheskinsecretionofhylaranaguentheri