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Evaluation of new cathepsin B inhibitors (585.2)
Author(s) -
Forgas David,
Wen Lisa,
Huang JenqKuen,
McConnell Rose
Publication year - 2014
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.28.1_supplement.585.2
Subject(s) - cathepsin b , cathepsin , cathepsin o , chemistry , cysteine protease , enzyme , biochemistry , proteases , microbiology and biotechnology , cancer research , pharmacology , medicine , biology
Cathepsin B, a cysteine protease that naturally occurs in human cells, is primarily responsible in protein degradation and bone resorption. However, Cathepsin B has been observed in excessive concentrations in patients suffering from certain cancers, as well as Alzheimer's Disease. Though the direct involvement of Cathepsin B within these cells is not currently known, the potential medical benefits of reducing Cathepsin B activities on these cells are promising. The purpose of this research was to evaluate the activity of 5 new synthetic inhibitors of Cathepsin B and to observe the effectiveness of each inhibitor by determining their half maximal inhibitory concentration (IC 50 ). Effectiveness of each inhibitor was determined by the enzyme's ability to cleave the chromogenic substrate, N‐Carbobenzoxy‐L‐Phenylalanyl‐Arginine‐4‐nitroanilide hydrochloride. The activity of the enzyme was observed at 405 nm over a span of 3 minutes. A dose‐response curve was then constructed to interpret the results. The benefits of this research could possibly pave the way for future anti‐cancer treatments, as well as other diseases characterized by over‐expression of cathepsin B. Grant Funding Source : National Cancer Institute at NIH (Grant No. 3R15CA086933‐04 and 3R15CA086933‐04A2S1) and WIU