2. Academic Validation
  3. Structure based development of novel specific inhibitors for cathepsin L and cathepsin S in vitro and in vivo

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. doi: 10.1016/s0014-5793(99)01107-2.
N Katunuma 1,  E Murata,  H Kakegawa,  A Matsui,  H Tsuzuki,  H Tsuge,  D Turk,  V Turk,  M Fukushima,  Y Tada,  T Asao
Affiliations

Affiliation

  • 1 Institute for Health Sciences, Tokushima Bunri University, Japan.
PMID: 10518923 DOI: 10.1016/s0014-5793(99)01107-2
Abstract

Specific inhibitors for Cathepsin L and Cathepsin S have been developed with the help of computer-graphic modeling based on the stereo-structure. The common fragment, N-(L-trans-carbamoyloxyrane-2-carbonyl)-phenylalanine-dimethyla mide, is required for specific inhibition of Cathepsin L. Seven novel inhibitors of the Cathepsin L Inhibitor Katunuma (CLIK) specifically inhibited Cathepsin L at a concentration of 10(-7) M in vitro, while almost no inhibition of cathepsins B, C, S and K was observed. Four of the CLIKs are stable, and showed highly selective inhibition for hepatic Cathepsin L in vivo. One of the CLIK inhibitors contains an aldehyde group, and specifically inhibits Cathepsin S at 10(-7) M in vitro.

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