Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity

Hydrophobicity and charge are key properties of antimicrobial peptides (AMPs). We compared the self-assembly performance and its correlation with antimicrobial activity of a designer AMP and analogues with substitution of hydrophobic or cationic residues by alanine. Peptides that formed supramolecul...

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Detalles Bibliográficos
Autores principales: Ye, Zhou, Aparicio, Conrado
Formato: Online Artículo Texto
Lenguaje:English
Publicado: RSC 2019
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6913536/
https://www.ncbi.nlm.nih.gov/pubmed/31844837
http://dx.doi.org/10.1039/c9na00498j
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author Ye, Zhou
Aparicio, Conrado
author_facet Ye, Zhou
Aparicio, Conrado
author_sort Ye, Zhou
collection PubMed
description Hydrophobicity and charge are key properties of antimicrobial peptides (AMPs). We compared the self-assembly performance and its correlation with antimicrobial activity of a designer AMP and analogues with substitution of hydrophobic or cationic residues by alanine. Peptides that formed supramolecular self-assemblies under the studied conditions were those that have higher antimicrobial potency.
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spelling pubmed-69135362019-12-16 Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity Ye, Zhou Aparicio, Conrado Nanoscale Adv Chemistry Hydrophobicity and charge are key properties of antimicrobial peptides (AMPs). We compared the self-assembly performance and its correlation with antimicrobial activity of a designer AMP and analogues with substitution of hydrophobic or cationic residues by alanine. Peptides that formed supramolecular self-assemblies under the studied conditions were those that have higher antimicrobial potency. RSC 2019-10-31 /pmc/articles/PMC6913536/ /pubmed/31844837 http://dx.doi.org/10.1039/c9na00498j Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Ye, Zhou
Aparicio, Conrado
Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity
title Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity
title_full Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity
title_fullStr Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity
title_full_unstemmed Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity
title_short Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity
title_sort modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6913536/
https://www.ncbi.nlm.nih.gov/pubmed/31844837
http://dx.doi.org/10.1039/c9na00498j
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