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Updated: Oct 14, 2025
Kinetic Screening of Nuclease Activity using Nucleic Acid Probes
Published on: November 1, 2019
Clickable, selective, and cell-permeable activity-based probe of human cathepsin B - Minimalistic approach for
Ashif I Bhuiyan1, Pratikkumar Rathod2, Sarbani Ghoshal3
1Queens College of The City University of New York, Chemistry and Biochemistry Department, 65-30 Kissena Blvd, Flushing, NY 11367, USA; Chemistry Doctoral Program, The Graduate Center of The City University of New York, 365 5th Ave, New York, NY 10016, USA.
Abstract:
Human cathepsin B is a cysteine-dependent protease whose roles in both normal and diseased cellular states remain yet to be fully delineated. This is primarily due to overlapping substrate specificities and lack of unambiguously annotated physiological functions. In this work, a selective, cell-permeable, clickable and tagless small molecule cathepsin B probe, KDA-1, is developed and kinetically characterized. KDA-1 selectively targets active site Cys25 residue of cathepsin B for labeling and can detect active cellular cathepsin B in proteomes derived from live human MDA-MB-231 breast cancer cells and HEK293 cells. It is anticipated that KDA-1 probe will find suitable applications in functional proteomics involving human cathepsin B enzyme.
