Structure based development of novel specific inhibitors for cathepsin L and cathepsin S in vitro and in vivo

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<jats:p>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, <jats:italic>N</jats:italic>‐(<jats:sc>L</jats:sc>‐<jats:italic>trans</jats:italic>‐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<jats:sup>−7</jats:sup> 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<jats:sup>−7</jats:sup> M in vitro.</jats:p>

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