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Title: Chemical biology of metalloproteases and cysteine proteases
Authors: HU MINGYU
Keywords: proteases, small molecules, inhibitor, probe, cell imaging
Issue Date: 14-Sep-2011
Citation: HU MINGYU (2011-09-14). Chemical biology of metalloproteases and cysteine proteases. ScholarBank@NUS Repository.
Abstract: Proteases are known to recognize a larger number of different substrates and are involved in almost every process in the cells. Abnormal proteases activities are linked to many serious diseases, such as cancer, inflammation, arteriosclerosis, neurodegeneration and infection. Due to their essential roles in physiological and pathological events, proteases are very important targets for drug development. Therefore, it will be interesting to establish a chemical biology platform to study and understand the activities, localizations and functions of different enzymes. In this thesis, we report a high-throughput strategy for assembling and in-situ screening of small molecule-based MMP inhibitors. A ?one-pot? click chemistry protocol was developed for this application. Furthermore, we also successfully developed fluorescent quenched activity-based probes suitable for biomedical applications. This approach provides real-time imaging of endogenous Caspase-3/7 activities in the apoptotic cells and could potentially target different classes of enzymes including glycosidases, phosphatases and various proteases.
Appears in Collections:Ph.D Theses (Open)

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