Phosphinic peptides as zinc metalloproteinase inhibitors
β Scribed by V. Dive; D. Georgiadis; M. Matziari; A. Makaritis; F. Beau; P. Cuniasse; A. Yiotakis
- Publisher
- Springer
- Year
- 2004
- Tongue
- English
- Weight
- 350 KB
- Volume
- 61
- Category
- Article
- ISSN
- 1420-682X
No coin nor oath required. For personal study only.
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The matrix metalloproteinase stromelysin-1 (MMP-3) is inhibited more strongly by peptidyl phosphinic acid 7 than by its corresponding phosphonamidate and phosphonate analogs. Extending a benzyl group at PI' to a phenylethyl group in 8 further increases the potency (Ki = 1.4 nM). Enhanced potency wit
## Abstract The __in vivo__ disposition and antitumor efficacy of a newly developed phosphinic matrix metalloproteinase inhibitor (RXP03) were examined. RXP03 potently inhibits MMPβ11, MMPβ8 and MMPβ13, but not MMPβ1 and MMPβ7. Twentyβfour hours after i.p. injection into mice, most of the RXP03 was