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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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Publication details

The article was received on 12 Aug 2019, accepted on 30 Oct 2019 and first published on 31 Oct 2019


Article type: Communication
DOI: 10.1039/C9NA00498J
Nanoscale Adv., 2019, Advance Article
  • Open access: Creative Commons BY-NC license
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    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, Advance Article , DOI: 10.1039/C9NA00498J

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