Journal article

New strategy for selective and sensitive assay of cathepsin B using a dityrosine-based material.

Chan-Jin Kim, Dong-Ik Lee, Dong Zhang, Chang-Ha Lee, Ik-Sung Ahn

Anal Biochem | Elsevier BV | Published : 2013

Abstract

The increasing number of reports for disease-related proteases has necessitated materials for the fast, sensitive, and specific assessment of protease activities. The purpose of this study was to synthesize and test a dityrosine-based substrate for the selective assay of a specific cysteine cathepsin. DBDY-Gly-INH)2 was synthesized from the conjugation of N,N'-diBoc-dityrosine (DBDY) with two molecules of glycine and isoniazid (INH) for this purpose. The fluorescence of DBDY (λex=284-320nm, λem=400-420nm) disappeared due to the quenching effect of INH. However, the protease-catalyzed hydrolysis resulted in the release of INH and recovered the fluorescence of DBDY. When reacted with 13 protea..

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University of Melbourne Researchers