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Targeted Modification and Structure-Activity Study of GL-29, an Analogue of the Antimicrobial Peptide Palustrin-2ISb

Antimicrobial peptides (AMPs) are considered as promising antimicrobial agents due to their potent bioactivity. Palustrin-2 peptides were previously found to exhibit broad-spectrum antimicrobial activity with low haemolytic activity. Therefore, GL-29 was used as a template for further modification a...

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Autores principales: Liu, Siyan, Lin, Yaxian, Liu, Jiachen, Chen, Xiaoling, Ma, Chengbang, Xi, Xinping, Zhou, Mei, Chen, Tianbao, Burrows, James F., Wang, Lei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9405102/
https://www.ncbi.nlm.nih.gov/pubmed/36009917
http://dx.doi.org/10.3390/antibiotics11081048
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author Liu, Siyan
Lin, Yaxian
Liu, Jiachen
Chen, Xiaoling
Ma, Chengbang
Xi, Xinping
Zhou, Mei
Chen, Tianbao
Burrows, James F.
Wang, Lei
author_facet Liu, Siyan
Lin, Yaxian
Liu, Jiachen
Chen, Xiaoling
Ma, Chengbang
Xi, Xinping
Zhou, Mei
Chen, Tianbao
Burrows, James F.
Wang, Lei
author_sort Liu, Siyan
collection PubMed
description Antimicrobial peptides (AMPs) are considered as promising antimicrobial agents due to their potent bioactivity. Palustrin-2 peptides were previously found to exhibit broad-spectrum antimicrobial activity with low haemolytic activity. Therefore, GL-29 was used as a template for further modification and study. Firstly, the truncated analogue, GL-22, was designed to examine the function of the ‘Rana box’, which was confirmed to have no impact on antimicrobial activity. The results of antimicrobial activity assessment against seven microorganisms demonstrated GL-22 to have a broad-spectrum antimicrobial activity, but weak potency against Candida albicans (C. albicans). These data were similar to those of GL-29, but GL-22 showed much lower haemolysis and lower cytotoxicity against HaCaT cells. Moreover, GL-22 exhibited potent in vivo activity at 4 × MIC against Staphylococcus aureus (S. aureus)-infected larvae. Several short analogues, from the C-terminus and N-terminus of GL-22, were modified to identify the shortest functional motif. However, the results demonstrated that the shorter peptides did not exhibit potent antimicrobial activity, and the factors that affect the bioactive potency of these short analogues need to be further studied.
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spelling pubmed-94051022022-08-26 Targeted Modification and Structure-Activity Study of GL-29, an Analogue of the Antimicrobial Peptide Palustrin-2ISb Liu, Siyan Lin, Yaxian Liu, Jiachen Chen, Xiaoling Ma, Chengbang Xi, Xinping Zhou, Mei Chen, Tianbao Burrows, James F. Wang, Lei Antibiotics (Basel) Article Antimicrobial peptides (AMPs) are considered as promising antimicrobial agents due to their potent bioactivity. Palustrin-2 peptides were previously found to exhibit broad-spectrum antimicrobial activity with low haemolytic activity. Therefore, GL-29 was used as a template for further modification and study. Firstly, the truncated analogue, GL-22, was designed to examine the function of the ‘Rana box’, which was confirmed to have no impact on antimicrobial activity. The results of antimicrobial activity assessment against seven microorganisms demonstrated GL-22 to have a broad-spectrum antimicrobial activity, but weak potency against Candida albicans (C. albicans). These data were similar to those of GL-29, but GL-22 showed much lower haemolysis and lower cytotoxicity against HaCaT cells. Moreover, GL-22 exhibited potent in vivo activity at 4 × MIC against Staphylococcus aureus (S. aureus)-infected larvae. Several short analogues, from the C-terminus and N-terminus of GL-22, were modified to identify the shortest functional motif. However, the results demonstrated that the shorter peptides did not exhibit potent antimicrobial activity, and the factors that affect the bioactive potency of these short analogues need to be further studied. MDPI 2022-08-03 /pmc/articles/PMC9405102/ /pubmed/36009917 http://dx.doi.org/10.3390/antibiotics11081048 Text en © 2022 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
Liu, Siyan
Lin, Yaxian
Liu, Jiachen
Chen, Xiaoling
Ma, Chengbang
Xi, Xinping
Zhou, Mei
Chen, Tianbao
Burrows, James F.
Wang, Lei
Targeted Modification and Structure-Activity Study of GL-29, an Analogue of the Antimicrobial Peptide Palustrin-2ISb
title Targeted Modification and Structure-Activity Study of GL-29, an Analogue of the Antimicrobial Peptide Palustrin-2ISb
title_full Targeted Modification and Structure-Activity Study of GL-29, an Analogue of the Antimicrobial Peptide Palustrin-2ISb
title_fullStr Targeted Modification and Structure-Activity Study of GL-29, an Analogue of the Antimicrobial Peptide Palustrin-2ISb
title_full_unstemmed Targeted Modification and Structure-Activity Study of GL-29, an Analogue of the Antimicrobial Peptide Palustrin-2ISb
title_short Targeted Modification and Structure-Activity Study of GL-29, an Analogue of the Antimicrobial Peptide Palustrin-2ISb
title_sort targeted modification and structure-activity study of gl-29, an analogue of the antimicrobial peptide palustrin-2isb
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9405102/
https://www.ncbi.nlm.nih.gov/pubmed/36009917
http://dx.doi.org/10.3390/antibiotics11081048
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