Cross‐Linking Yield Variation of a Potent Matrix Metalloproteinase Photoaffinity Probe and Consequences for Functional Proteomics | Zendy

David Arnaud | Zendy; Steer David | Zendy; Bregant Sarah | Zendy; Devel Laurent | Zendy; Makaritis Anastasios | Zendy; Beau Fabrice | Zendy; Yiotakis Athanasios | Zendy; Dive Vincent | Zendy

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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.

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