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Kinetic studies of synthetic argininal thiosemicarbazone containing inhibitors of cathepsin B
Author(s) -
Wen Lisa,
Yelma Niranjan Reddy,
Lucas Joseph,
Huang JenqKuen,
McConnell Rose
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.560.9
Subject(s) - cathepsin b , cathepsin , chemistry , cysteine protease , cancer , enzyme , metastasis , cancer research , biochemistry , protease , apoptosis , microbiology and biotechnology , pharmacology , biology , medicine
Cathepsin B, a lysosomal cysteine protease, plays roles in diverse cellular processes including protein degradation, antigen processing, and apoptosis. It has been implicated in many diseases such as cancer invasion and metastasis, inflammation, and Alzheimer's Disease. Thus, cathepsin B is a promising target for the development of therapeutic agents for treatment of many types of cancer and Alzheimer's Disease. Previously prepared synthetic argininal thiosemicarbazone containing inhibitors were evaluated for their ability to inhibit recombinant human cathepsin B by determining their IC 50 values. The studies were performed by colorimetric enzyme inhibition assay using N‐Carbobenzoxy‐L‐Phenylalanyl‐Arginine‐4‐nitroanilide hydrochloride as the chromogenic substrate. Kinetic properties of four potential inhibitors were characterized. Funding provided by National Cancer Institute at NIH (Grant No. 3R15CA086933–04 and 3R15CA086933–04A2S1) and Western Illinois University.