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

Zhou Ye, Xiao Zhu, Sergio Acosta, Dhiraj Kumar, Ting Sang, Conrado Aparicio

Research output: Contribution to journalArticle

17 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)266-275
Number of pages10
Issue number1
StatePublished - Jan 7 2019

PubMed: MeSH publication types

  • Journal Article

Fingerprint Dive into the research topics of 'Self-assembly dynamics and antimicrobial activity of all l- and d-amino acid enantiomers of a designer peptide'. Together they form a unique fingerprint.

  • Cite this