(R)-α-Trifluoromethylalanine as a 19F NMR Probe for the Monitoring of Protease Digestion of Peptides

被引:6
|
作者
Devillers, Emmanuelle [1 ,2 ]
Chelain, Evelyne [1 ,2 ]
Dalvit, Claudio [3 ,4 ]
Brigaud, Thierry [1 ,2 ]
Pytkowicz, Julien [1 ,2 ]
机构
[1] CY Cergy Paris Univ, CNRS, BIOCIS, 5 Mail Gay Lussac, F-95031 Neuville Sur Oise, Cergy Pontoise, France
[2] Univ Paris Saclay, BIOCIS, CNRS, F-92290 Chatenay Malabry, France
[3] Univ Neuchatel, Fac Sci, Ave Bellevaux 51, CH-2000 Neuchatel, Switzerland
[4] Lavis, Trento, Italy
关键词
FABS; NMR spectroscopy; pepsin; trifluoromethylated peptides; trypsin; PROTEOLYTIC STABILITY; PROLYL OLIGOPEPTIDASE; VERSATILE TOOL; LABEL; IDENTIFICATION; THERAPEUTICS; CHYMOTRYPSIN; FLUORINATION; EFFICIENT; DESIGN;
D O I
10.1002/cbic.202100470
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Fluorinated non-natural amino acids are useful tools for improving the bioavailability of peptides but can also serve as fluorinated probes in F-19 NMR-based enzymatic assays. We report herein that the use of the non-natural alpha-quaternarized (R)-alpha-trifluoromethylalanine ((R)-alpha-TfmAla) provides convenient and accurate monitoring of trypsin proteolytic activity and increases resistance towards pepsin degradation.
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页数:5
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