(R)‐α‐Trifluoromethylalanine as a 19F NMR Probe for the Monitoring of Protease Digestion of Peptides. (18th November 2021)

• Record Type: Journal Article
• Authors: Devillers, Emmanuelle; Chelain, Evelyne; Dalvit, Claudio; Brigaud, Thierry; Pytkowicz, Julien
• Is Part Of: Chembiochem. Volume 23:Number 1(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2021-11-18
• Subjects: FABS -- NMR spectroscopy -- pepsin -- trifluoromethylated peptides -- trypsin; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.202100470
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Fluorinated non‐natural amino acids are useful tools for improving the bioavailability of peptides but can also serve as fluorinated probes in 19 F NMR‐based enzymatic assays. We report herein that the use of the non‐natural α‐quaternarized ( R )‐α‐trifluoromethylalanine (( R )‐α‐TfmAla) provides convenient and accurate monitoring of trypsin proteolytic activity and increases resistance towards pepsin degradation. Abstract : A useful fluorinated NMR probe : α‐Quaternarized ( R )‐α‐trifluoromethylalanine (α‐TfmAla) is a good tool for providing convenient and accurate 19 F NMR‐based monitoring of trypsin proteolytic activity and increases resistance towards pepsin degradation.