A rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.

Linear cationic α-helical antimicrobial peptides are referred to as one of the most likely substitutes for common antibiotics, due to their relatively simple structures (≤ 40 residues) and various antimicrobial activities against a wide range of pathogens. Of those, HP(2-20) was isolated from Helico...

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Autores principales:	Li Liu, Ying Fang, Qingsheng Huang, Jianhua Wu
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2928db0ebce849559df626d52b76acf7
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spelling	oai:doaj.org-article:2928db0ebce849559df626d52b76acf72021-11-18T07:00:01ZA rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.1932-620310.1371/journal.pone.0016441https://doaj.org/article/2928db0ebce849559df626d52b76acf72011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21283643/?tool=EBIhttps://doaj.org/toc/1932-6203Linear cationic α-helical antimicrobial peptides are referred to as one of the most likely substitutes for common antibiotics, due to their relatively simple structures (≤ 40 residues) and various antimicrobial activities against a wide range of pathogens. Of those, HP(2-20) was isolated from Helicobacter pylori ribosomal protein. To reveal a mechanical determinant that may mediate the antimicrobial activities, we examined the mechanical properties and structural stabilities of HP(2-20) and its four analogues of same chain length by steered molecular dynamics simulation. The results indicated the following: the resistance of H-bonds to the tensile extension mediated the early extensive stage; with the loss of H-bonds, the tensile force was dispensed to prompt the conformational phase transition; and Young's moduli (N/m(2)) of the peptides were about 4 ∼ 8 × 10(9). These mechanical features were sensitive to the variation of the residue compositions. Furthermore, we found that the antimicrobial activity is rigidity-enhanced, that is, a harder peptide has stronger antimicrobial activity. It suggests that the molecular spring constant may be used to seek a new structure-activity relationship for different α-helical peptide groups. This exciting result was reasonably explained by a possible mechanical mechanism that regulates both the membrane pore formation and the peptide insertion.Li LiuYing FangQingsheng HuangJianhua WuPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 1, p e16441 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Li Liu Ying Fang Qingsheng Huang Jianhua Wu A rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.
description	Linear cationic α-helical antimicrobial peptides are referred to as one of the most likely substitutes for common antibiotics, due to their relatively simple structures (≤ 40 residues) and various antimicrobial activities against a wide range of pathogens. Of those, HP(2-20) was isolated from Helicobacter pylori ribosomal protein. To reveal a mechanical determinant that may mediate the antimicrobial activities, we examined the mechanical properties and structural stabilities of HP(2-20) and its four analogues of same chain length by steered molecular dynamics simulation. The results indicated the following: the resistance of H-bonds to the tensile extension mediated the early extensive stage; with the loss of H-bonds, the tensile force was dispensed to prompt the conformational phase transition; and Young's moduli (N/m(2)) of the peptides were about 4 ∼ 8 × 10(9). These mechanical features were sensitive to the variation of the residue compositions. Furthermore, we found that the antimicrobial activity is rigidity-enhanced, that is, a harder peptide has stronger antimicrobial activity. It suggests that the molecular spring constant may be used to seek a new structure-activity relationship for different α-helical peptide groups. This exciting result was reasonably explained by a possible mechanical mechanism that regulates both the membrane pore formation and the peptide insertion.
format	article
author	Li Liu Ying Fang Qingsheng Huang Jianhua Wu
author_facet	Li Liu Ying Fang Qingsheng Huang Jianhua Wu
author_sort	Li Liu
title	A rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.
title_short	A rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.
title_full	A rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.
title_fullStr	A rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.
title_full_unstemmed	A rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.
title_sort	rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide hp(2-20) and its four analogues.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/2928db0ebce849559df626d52b76acf7
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A rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.

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