Premium
Cross‐Linking Yield Variation of a Potent Matrix Metalloproteinase Photoaffinity Probe and Consequences for Functional Proteomics
Author(s) -
David Arnaud,
Steer David,
Bregant Sarah,
Devel Laurent,
Makaritis Anastasios,
Beau Fabrice,
Yiotakis Athanasios,
Dive Vincent
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200604408
Subject(s) - matrix metalloproteinase , yield (engineering) , photoaffinity labeling , chemistry , in vitro , matrix (chemical analysis) , computational biology , combinatorial chemistry , biophysics , biochemistry , binding site , chromatography , biology , materials science , metallurgy
Probing proteinases : A radioactive photoaffinity probe exhibiting subnanomolar potency towards matrix metalloproteinases (MMPs) has been developed (see structure). High sensitivity in the detection of particular MMPs has been obtained; however, high variation in the cross‐linking yield of MMPs with this probe may limit its ability to detect all MMP active forms in biological samples. This result suggests that a cocktail of optimized probes should be developed.