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Issue 12, 2019
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Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity

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Abstract

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.

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

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Supplementary files

Article information


Submitted
12 Aug 2019
Accepted
30 Oct 2019
First published
31 Oct 2019

This article is Open Access

Nanoscale Adv., 2019,1, 4679-4682
Article type
Communication

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

Z. Ye and C. Aparicio, Nanoscale Adv., 2019, 1, 4679
DOI: 10.1039/C9NA00498J

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