215098-90-1
Chemical Structure
CLIK-148
- CAS No.: 215098-90-1
- Formula:C22H26N4O4
- Molecular Weight:410.47
InChIKey: SXMRSAGDCJGMTG-FHWLQOOXSA-N
SMILES: CN(C)C([C@H](CC1=CC=CC=C1)NC([C@@H]2[C@H](O2)C(NCCC3=CC=CC=N3)=O)=O)=O
Biological Activity: CLIK-148 is a highly selective, irreversible and orally active cysteine protease inhibitor, primarily targeting Cathepsin L. CLIK-148 effectively inhibits the Cathepsin L-dependent degradation of HMG-CoA reductase in the endoplasmic reticulum (ER) membrane. CLIK-148 inhibits the processing of proCCK by Cathepsin L, thereby reducing the production of CCK8 (HY-P0093). CLIK-148 inhibits the degradation of type I collagen by osteoclasts' secreted Cathepsin L, reducing tumor-induced bone metastasis and malignant hypercalcemia. CLIK-148 can be used for the studies of bone metabolism disorders and regulation of neuropeptide processing[1][2][3][4].
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CLIK-148 | CLIK-148 is a highly selective, irreversible and orally active cysteine protease inhibitor, primarily targeting Cathepsin L. CLIK-148 effectively inhibits the Cathepsin L-dependent degradation of HMG-CoA reductase in the endoplasmic reticulum (ER) membrane. CLIK-148 inhibits the processing of proCCK by Cathepsin L, thereby reducing the production of CCK8 (HY-P0093). CLIK-148 inhibits the degradation of type I collagen by osteoclasts' secreted Cathepsin L, reducing tumor-induced bone metastasis and malignant hypercalcemia. CLIK-148 can be used for the studies of bone metabolism disorders and regulation of neuropeptide processing. | |||||||||||||||||||||
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References
- [1]. Katunuma N, et al. Structure based development of novel specific inhibitors for cathepsin L and cathepsin S in vitro and in vivo. FEBS Lett. 1999 Sep 10;458(1):6-10. [Content Brief]
- [2]. Beinfeld MC, et al. Cathepsin L plays a major role in cholecystokinin production in mouse brain cortex and in pituitary AtT-20 cells: protease gene knockout and inhibitor studies. Peptides. 2009 Oct;30(10):1882-91. [Content Brief]
- [3]. Katunuma N, et al. Structure-based design of specific cathepsin inhibitors and their application to protection of bone metastases of cancer cells. Arch Biochem Biophys. 2002 Jan 15;397(2):305-11. [Content Brief]
- [4]. Moriyama T, et al. 3-hydroxy-3-methylglutaryl coenzyme A reductase is sterol-dependently cleaved by cathepsin L-type cysteine protease in the isolated endoplasmic reticulum. Arch Biochem Biophys. 2001 Feb 15;386(2):205-12. [Content Brief]
