The role of β-hairpin conformation in ester hydrolysis peptide catalysts based on a TrpZip scaffold.

Autor: Liu X; Department of Chemistry, University of Wisconsin-Madison Madison Wisconsin 53706 USA., Waters R; Department of Chemistry, Macalester College Saint Paul Minnesota 55105 USA lwitus@macalester.edu., Gilbert HE; Department of Chemistry, Macalester College Saint Paul Minnesota 55105 USA lwitus@macalester.edu., Barroso GT; Department of Chemistry, Macalester College Saint Paul Minnesota 55105 USA lwitus@macalester.edu., Boyle KM; Department of Chemistry, Macalester College Saint Paul Minnesota 55105 USA lwitus@macalester.edu., Witus LS; Department of Chemistry, Macalester College Saint Paul Minnesota 55105 USA lwitus@macalester.edu.
Jazyk: angličtina
Zdroj: RSC advances [RSC Adv] 2021 Jul 06; Vol. 11 (38), pp. 23714-23718. Date of Electronic Publication: 2021 Jul 06 (Print Publication: 2021).
DOI: 10.1039/d1ra04288b
Abstrakt: To explore the role of peptide conformation on catalytic activity in the context of ester hydrolysis catalysts, pairs of sequences were designed that contained or lacked β-hairpin character. For the hydrolysis of para -nitrophenylacetate in aqueous media, we found small but consistent trends wherein His-containing sequences based on a TrpZip scaffold showed higher catalytic activity without β-hairpin character.
Competing Interests: There are no conflicts to declare.
(This journal is © The Royal Society of Chemistry.)
Databáze: MEDLINE