Conformational Study of an Artificial Metal-Dependent Regulation Site for Use in Designer Proteins.

ABSTRACT: This report describes the dimerisation of glutathione, and by extension, other cysteine-containing peptides or protein fragments, with a 5, 5'-disubstituted-2, 2'-bipyridine or 6, 6"-disubstituted-2, 2':6',2"-terpyridine unit. The resulting bipy-GS₂ and terpy-GS₂ were investigated as potential metal ion dependent switches in aqueous solution, and were found to predominantly adopt the transoïd conformation at physiological pH. Metal complexation with Cu^II and Zn^II at this pH has been studied by UV/Vis, CD, NMR and ion-mobility mass spectrometry. Zn^II titrations are consistent with the formation of a 1:1 Zn^II:terpy-GS₂ complex at pH 7.4, but bipy-GS₂

SUBMITTER: Oheix E 

PROVIDER: S-EPMC4431501 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature