132259-06-4
Chemical Structure
RP 59794
- CAS No.: 132259-06-4
- Formula:C20H31N3O4
- Molecular Weight:377.48
InChIKey: XYFQZHLDJQWPJJ-FUHWJXTLSA-N
SMILES: O=C(NCC1=CC=CC=C1)[C@@H](C(C)C)NC([C@@H](CC(C)C)CC(NO)=O)=O
Biological Activity: RP 59794 is a potent collagenase (collagenase) and broad-spectrum matrix metalloproteinase (MMP) inhibitor. The active stereoisomer of RP 59794 has a Ki of 13 nM against MMP-1 (with native collagen as substrate) and 45 nM (with a synthetic octapeptide as substrate). RP 59794 blocks and partially dissociates TIMP by binding to the active site of collagenase, specifically inhibits the collagen-transmigrating migration of osteoclasts and bone resorption on collagen-coated surfaces, but exerts no effect on cell migration in collagen-free environments, and acts in a time-dependent manner in bone tissues. RP 59794 can be used in studies of arthritis, periodontal disease, corneal ulcers and tumor invasion[1][2][3].
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RP 59794 | RP 59794 is a potent collagenase (collagenase) and broad-spectrum matrix metalloproteinase (MMP) inhibitor. The active stereoisomer of RP 59794 has a Ki of 13 nM against MMP-1 (with native collagen as substrate) and 45 nM (with a synthetic octapeptide as substrate). RP 59794 blocks and partially dissociates TIMP by binding to the active site of collagenase, specifically inhibits the collagen-transmigrating migration of osteoclasts and bone resorption on collagen-coated surfaces, but exerts no effect on cell migration in collagen-free environments, and acts in a time-dependent manner in bone tissues. RP 59794 can be used in studies of arthritis, periodontal disease, corneal ulcers and tumor invasion. | |||||||||||||||||||||
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References
- [1]. Lelièvre Y, et al. Low molecular weight, sequence based, collagenase inhibitors selectively block the interaction between collagenase and TIMP (tissue inhibitor of metalloproteinases). Matrix (Stuttgart, Germany). 1990 Oct;10(5):292-9. [Content Brief]
- [2]. Sato T, et al. The migration of purified osteoclasts through collagen is inhibited by matrix metalloproteinase inhibitors. Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research. 1998 Jan;13(1):59-66. [Content Brief]
- [3]. Everts V, et al. Cysteine proteinases and matrix metalloproteinases play distinct roles in the subosteoclastic resorption zone. Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research. 1998 Sep;13(9):1420-30. [Content Brief]
