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Title: Chemical proteomics approaches to study aspartic and metalloproteases
Keywords: chemical proteomics, affinity-based profiling, aspartic protease, metalloprotease, click chemistry
Issue Date: 20-Nov-2004
Citation: CHAN WEN SHUN, ELAINE (2004-11-20). Chemical proteomics approaches to study aspartic and metalloproteases. ScholarBank@NUS Repository.
Abstract: A complementary chemical proteomics approach to the activity-based profiling strategy is described herein. Trifunctional probes, comprising of an affinity binding unit, a photolabile group and a fluorescent reporter tag, were designed for the affinity-based profiling of metalloproteases and aspartic proteases. Through a repertoire of labeling experiments, the ability of the probes to selectively and specifically capture the desired enzymes with minimal interference and background was adequately demonstrated, laying the framework for the use of affinity-based concept in large-scale proteomic profiling experiments. An analogous strategy akin to the dynamic combinatorial chemistry concept is also reported. A series of azide- and alkyne-bearing cores were prepared. Using recombinant HIV-1 protease as a host, the sequestering of the precursors in the active site of the enzyme resulted in the catalysis of the click chemistry ligation reaction due to proximity effects. The preliminary results obtained at this stage sets the groundwork for potential extension to complex systems involving multiple components.
Appears in Collections:Master's Theses (Open)

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