[HTML][HTML] Structure based development of novel specific inhibitors for cathepsin L and cathepsin S in vitro and in vivo
N Katunuma, E Murata, H Kakegawa, A Matsui… - FEBS letters, 1999 - Elsevier
N Katunuma, E Murata, H Kakegawa, A Matsui, H Tsuzuki, H Tsuge, D Turk, V Turk…
FEBS letters, 1999•ElsevierSpecific 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-dimethylamide, 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 …
computer-graphic modeling based on the stereo-structure. The common fragment, N-(L-
trans-carbamoyloxyrane-2-carbonyl)-phenylalanine-dimethylamide, 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 …
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-dimethylamide, 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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