Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/47624
Title: DESIGN, SYNTHESIS AND EVALUATION OF NEW PHOSPHOTYROSINE MIMICS
Authors: GE JINGYAN
Keywords: phosphotyrosine, mimic, phosphoproteomic, activity-based probe, PTP, catalomics
Issue Date: 27-Jun-2012
Source: GE JINGYAN (2012-06-27). DESIGN, SYNTHESIS AND EVALUATION OF NEW PHOSPHOTYROSINE MIMICS. ScholarBank@NUS Repository.
Abstract: Reversible protein phosphorylation plays a fundamental role in signal transduction. Protein phosphatases, protein kinases and some modular domains (SH2, PDB, etc) form key components of the highly complex human phosphoproteome network. Dysregulation of this network is known to cause many human diseases including cancer. The phosphotyrosine (pTyr) residue in a protein serves as one of the key recognition and binding elements for signaling proteins. Its hydrolytic instability and poor cell permeability has led to the development of many novel phosphate mimics. This thesis described several pTyr mimics, most of which possess suitable N- and C-terminus for conjugation/incorporation into peptide/protein synthesis, including 1) isoxazole carboxylic acid-based mimics that possess better cell permeability and hydrolytic stability; 2) quinone methide-based mimics containing fluorogenic and self-immobilizing properties; 3) vinyl sulfonate-based mimics having irreversible covalent labeling reactivity. These small pTyr mimics were subsequently incorporated into either small molecules or peptides to provide expanded chemical tools for further chemical biology applications, such as bioimaging, FACS and activity based-profiling. Furthermore, we successfully explored the multi-component Ugi reaction for rapid assembly of a panel of protein tyrosine phosphatase-targeting affinity-based probes (AfBPs).
URI: http://scholarbank.nus.edu.sg/handle/10635/47624
Appears in Collections:Ph.D Theses (Open)

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