Hydrolysis, polarity, and conformational impact of C-terminal partially fluorinated ethyl esters in peptide models.

ABSTRACT: Fluorinated moieties are highly valuable to chemists due to the sensitive NMR detectability of the 19F nucleus. Fluorination of molecular scaffolds can also selectively influence a molecule's polarity, conformational preferences and chemical reactivity, properties that can be exploited for various chemical applications. A powerful route for incorporating fluorine atoms in biomolecules is last-stage fluorination of peptide scaffolds. One of these methods involves esterification of the C-terminus of peptides using a diazomethane species. Here, we provide an investigation of the physicochemical consequences of peptide esterification with partially fluorinated ethyl groups. Derivatives of N-acetylproline are used to model the effects of fluorination on the lipophilicity, hydrolytic stability a

SUBMITTER: Kubyshkin V 

PROVIDER: S-EPMC5704756 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature