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Article: Modulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity

TitleModulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity
Authors
Ye, ZhouAparicio, Conrado
Issue Date2019
Citation
Nanoscale Advances, 2019, v. 1, n. 12, p. 4679-4682 How to Cite?
DOI: http://dx.doi.org/10.1039/c9na00498j
AbstractHydrophobicity 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.
Persistent Identifierhttp://hdl.handle.net/10722/318801
PubMed Central ID
PMC6913536
ISI Accession Number ID
WOS:000501347800008

 

DC FieldValueLanguage
dc.contributor.authorYe, Zhou-
dc.contributor.authorAparicio, Conrado-
dc.date.accessioned2022-10-11T12:24:35Z-
dc.date.available2022-10-11T12:24:35Z-
dc.date.issued2019-
dc.identifier.citationNanoscale Advances, 2019, v. 1, n. 12, p. 4679-4682-
dc.identifier.urihttp://hdl.handle.net/10722/318801-
dc.description.abstractHydrophobicity 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.-
dc.languageeng-
dc.relation.ispartofNanoscale Advances-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleModulation of supramolecular self-assembly of an antimicrobial designer peptide by single amino acid substitution: implications on peptide activity-
dc.typeArticle-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1039/c9na00498j-
dc.identifier.pmid31844837-
dc.identifier.pmcidPMC6913536-
dc.identifier.scopuseid_2-s2.0-85075970104-
dc.identifier.volume1-
dc.identifier.issue12-
dc.identifier.spage4679-
dc.identifier.epage4682-
dc.identifier.eissn2516-0230-
dc.identifier.isiWOS:000501347800008-

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