Please use this identifier to cite or link to this item:
Title: Organometallic Scaffolds as Protein Tyrosine Phosphatase 1B Inhibitor
Keywords: ruthenium, PTP-1B, TC-PTP, PTP, metalloinhibitor, diabetes
Issue Date: 24-Aug-2012
Source: ONG JUN XIANG (2012-08-24). Organometallic Scaffolds as Protein Tyrosine Phosphatase 1B Inhibitor. ScholarBank@NUS Repository.
Abstract: This thesis describes the synthesis of two novel classes of organo-ruthenium and organo-gold complexes as inhibitors of protein tyrosine phosphatases (PTPs). These organo-metallic complexes were rationally designed to be inhibitors of PTPs by attaching a non-hydrolyzable mimetic of phosphotyrosine to the ruthenium(II) and gold(I) metal centers respectively. The series of organo-ruthenium complexes have been found to inhibit protein tyrosine phosphatase 1B (PTP-1B) at low micromolar level with 7-10 fold selectivity towards PTP-1B over T-cell protein tyrosine phosphatase (TC-PTP). Molecular docking studies have also shown that the organo-ruthenium complexes bind better than the parent ligands in PTP-1B due to additional hydrophobic interactions with Phe182. These results suggest that this new class of organo-ruthenium complexes may be promising therapeutic agents to target PTP-1B. Similarly, one alkynyltriphenylphosphinegold(I) complex has been synthesized. Future work will include synthesizing a library of gold(I) complexes bearing a variety of phosphine ligands and evaluating these organo-gold(I) complexes as inhibitors of PTPs.
Appears in Collections:Master's Theses (Open)

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
OngJX.pdf2.5 MBAdobe PDF



Page view(s)

checked on Jan 12, 2018


checked on Jan 12, 2018

Google ScholarTM


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.