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Initial evaluation of the antitumour activity of KGP94, a functionalized benzophenone thiosemicarbazone inhibitor of cathepsin L.

Abstract：

:Kinetic analysis of the mode of inhibition of cathepsin L by KGP94, a lead compound from a privileged library of functionalized benzophenone thiosemicarbazone derivatives, demonstrated that it is a time-dependent, reversible, and competitive inhibitor of the enzyme. These results are consistent with the formation of a transient covalent bond, and are supported by molecular modeling that places the thiocarbonyl of the inhibitor in proximity to the thiolate moiety of the enzyme active site Cys25. KGP94 significantly decreased the activity of cathepsin L toward human type I collagen, and impeded both migration and invasion of MDA-MB-231 human breast cancer cells. Growth retardation was achieved in vivo against both recently implanted and established tumours using a C3H mouse mammary carcinoma model.

journal_name

Eur J Med Chem

journal_title

European journal of medicinal chemistry

authors

Chavarria GE,Horsman MR,Arispe WM,Kumar GD,Chen SE,Strecker TE,Parker EN,Chaplin DJ,Pinney KG,Trawick ML

doi

10.1016/j.ejmech.2012.10.039

subject

Has Abstract

pub_date

2012-12-01 00:00:00

pages

568-72

eissn

0223-5234

issn

1768-3254

pii

S0223-5234(12)00643-5

journal_volume

58

pub_type

杂志文章

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