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Self-assembly dynamics and antimicrobial activity of all L- and D-amino acid enantiomers of a designer peptide

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Abstract

Recent studies have shown that antimicrobial peptides (AMPs) can self-assemble into supramolecular structures, but this has been overlooked as causative of their antimicrobial activity. Also, the higher antimicrobial potency of D-enantiomers compared to L-enantiomers of AMPs cannot always be attributed to their different resistance to protease degradation. Here, we tested all L- and D-amino acid versions of GL13K, an AMP derived from a human protein, to study structural links between the AMP secondary structure, supramolecular self-assembly dynamics, and antimicrobial activity. pH dependence and the evolution of secondary structures were related to a self-assembly process with differences among these AMPs. The two GL13K enantiomers formed analogous self-assembled twisted nanoribbon structures, but D-GL13K initiated self-assembly faster and had notably higher antimicrobial potency than L-GL13K. A non-antimicrobial scrambled amino acid version of L-GL13K assembled at a much higher pH to form distinctively different self-assembled structures than L-GL13K. Our results support a functional relationship between the AMP self-assembly and their antimicrobial activity.

Graphical abstract: Self-assembly dynamics and antimicrobial activity of all l- and d-amino acid enantiomers of a designer peptide

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Publication details

The article was received on 10 Sep 2018, accepted on 20 Nov 2018 and first published on 21 Nov 2018


Article type: Paper
DOI: 10.1039/C8NR07334A
Citation: Nanoscale, 2019, Advance Article
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    Self-assembly dynamics and antimicrobial activity of all L- and D-amino acid enantiomers of a designer peptide

    Z. Ye, X. Zhu, S. Acosta, D. Kumar, T. Sang and C. Aparicio, Nanoscale, 2019, Advance Article , DOI: 10.1039/C8NR07334A

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