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

TitleSelf-assembly dynamics and antimicrobial activity of all l- and d-amino acid enantiomers of a designer peptide
Authors
Issue Date2019
Citation
Nanoscale, 2019, v. 11, n. 1, p. 266-275 How to Cite?
AbstractRecent 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.
Persistent Identifierhttp://hdl.handle.net/10722/318749
ISSN
2023 Impact Factor: 5.8
2023 SCImago Journal Rankings: 1.416
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYe, Zhou-
dc.contributor.authorZhu, Xiao-
dc.contributor.authorAcosta, Sergio-
dc.contributor.authorKumar, Dhiraj-
dc.contributor.authorSang, Ting-
dc.contributor.authorAparicio, Conrado-
dc.date.accessioned2022-10-11T12:24:28Z-
dc.date.available2022-10-11T12:24:28Z-
dc.date.issued2019-
dc.identifier.citationNanoscale, 2019, v. 11, n. 1, p. 266-275-
dc.identifier.issn2040-3364-
dc.identifier.urihttp://hdl.handle.net/10722/318749-
dc.description.abstractRecent 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.-
dc.languageeng-
dc.relation.ispartofNanoscale-
dc.titleSelf-assembly dynamics and antimicrobial activity of all l- and d-amino acid enantiomers of a designer peptide-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1039/c8nr07334a-
dc.identifier.pmid30534763-
dc.identifier.scopuseid_2-s2.0-85058870714-
dc.identifier.volume11-
dc.identifier.issue1-
dc.identifier.spage266-
dc.identifier.epage275-
dc.identifier.eissn2040-3372-
dc.identifier.isiWOS:000454327500022-

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