Cross-linking yield variation of a potent matrix metalloproteinase photoaffinity probe and consequences for functional proteomics

被引：34

作者：

David, Arnaud

Steer, David

Bregant, Sarah

Devel, Laurent

Makaritis, Anastasios

Beau, Fabrice

Yiotakis, Athanasios

Dive, Vincent ^{[1
]}

机构：

[1] CEA, IBITECS, SIMOPRO, F-91191 Gif Sur Yvette, France

[2] Univ Athens, Organ Chem Lab, GR-15771 Athens, Greece

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2007年 / 46卷 / 18期

关键词：

inhibitors; metalloproteinases; photoaffinity probes; protein profiling; proteomics;

D O I：

10.1002/anie.200604408

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Chemical Equation Presented) 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. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：3275 / 3277

页数：3

共 19 条

[1] Developing photoactive affinity probes for proteomic profiling: Hydroxamate-based probes for metalloproteases [J].