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.

Original languageEnglish (US)
Pages (from-to)4679-4682
Number of pages4
JournalNanoscale Advances
Volume1
Issue number12
DOIs
StatePublished - 2019

Bibliographical note

Funding Information:
We acknowledge Dr Sven-U. Gorr, University of Minnesota for generously donating all GL13K analogues and fruitful discussions about the antimicrobial activity of GL13K peptides. We also thank Erik Skoe for language editing of the manuscript. This work was supported by the National Institute for Dental and Craniofacial Research of the National Institutes of Health [grant number R01DE026117 to C. A.]. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. Parts of this work were carried out in the University of Minnesota I.T. Characterization Facility, which receives partial support from NSF through the MRSEC program.

Publisher Copyright:
© 2019 The Royal Society of Chemistry.

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