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

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.

SUBMITTER: Ye Z

PROVIDER: S-EPMC6913536 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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

Ye Zhou Z Aparicio Conrado C

Nanoscale advances 20191031 12

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. ...[more]

PMID: 31844837

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