350697-41-5Relevant academic research and scientific papers
Heterocycle-based MMP inhibitors with P2′ substituents
Pikul, Stanislaw,Dunham, Kelly McDow,Almstead, Neil G,De, Biswanath,Natchus, Michael G,Taiwo, Yetunde O,Williams, Lisa E,Hynd, Barbara A,Hsieh, Lily C,Janusz, Michael J,Gu, Fei,Mieling, Glen E
, p. 1009 - 1013 (2007/10/03)
Potent and selective inhibition of matrix metalloproteinases was demonstrated for a series of sulfonamide-based hydroxamic acids. The design of the heterocyclic sulfonamides incorporates a six- or seven-member central ring with a P2′ substituent that can be modified. Binding interactions of this substituent at the S2′ site are believed to contribute to high inhibitory potency against stromelysin, collagenase-3 and gelatinases A and B, and to provide selectivity against collagenase-1 and matrilysin. An X-ray structure of a stromelysin-inhibitor complex was obtained to provide insights into the SAR and selectivity trends observed for the series.
