@article{3027090, title = "A Pan Photoaffinity Probe for Detecting Active Forms of Matrix Metalloproteinases", author = "Nury, C. and Czarny, B. and Cassar-Lajeunesse, E. and Georgiadis, D. and Bregant, S. and Dive, V.", journal = "ChemBioChem", year = "2013", volume = "14", number = "1", pages = "107-114", issn = "1439-4227, 1439-7633", doi = "10.1002/cbic.201200583", keywords = "collagenase 3; gelatinase A; gelatinase B; macrophage elastase; matrix metalloproteinase; matrix metalloproteinase 14; neutrophil collagenase; stromelysin; tritium, article; chemical modification; controlled study; cross linking; enzyme mechanism; photoaffinity labeling; priority journal; radioactivity; radiography, Azides; Azirines; Catalytic Domain; Cross-Linking Reagents; Humans; Light; Matrix Metalloproteinases; Molecular Probe Techniques; Photoaffinity Labels", abstract = "A photoaffinity probe based on the scaffold of a potent broad-spectrum phosphinic peptide inhibitor of matrix metalloproteinases (MMPs) has been developed. A photolabile diazirine group for covalent modification of MMP active forms was incorporated at the P1′ position, and a tritium radioactive label for the sensitive detection of MMP covalent adducts by radioimaging was attached. The probe was characterized on seven catalytic domains of human MMPs (MMP-2, -3, -8, -9, -12, -13 and -14) and was found to display nanomolar affinities towards this set of MMPs, covalently modifying them with crosslinking yields varying from 12 to 58%, thus leading to highly sensitive detection of these MMPs. In a complex proteome complemented with four recombinant MMPs (MMP-2, -9, -12 and -13), this probe enabled their simultaneous detection with a threshold of few femtomoles and low background labelling. Those properties should make this new pan-activity-based MMP probe a valuable tool for the detection of MMP active forms from biological fluids or tissue extracts. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim." }