Low molecular weight protein tyrosine phosphatases (LMW-PTPs) are enzymes that have been linked to cellular transformation.  In addition, the overexpression of LMW-PTP in tumor cells has been recently shown to induce neoplasticity in nontransforrmed cells. Furthermore, LMW-PTP human isoform B has been demonstrated to be oncogenic. The docking of pyridoxal 5'-phosphate (PLP), a strong competitive inhibitor of LMW-PTP, with LMW-PTP isoform B was examined.  Phosphonate analogs of pyridoxamine, where the aminomethyl group is modified with different aromatic groups and the 5'-position converted to a phosphonic acid group, were screened virtually.  These analogs were then synthesized and tested via an in vitro kinetic assay with LMW-PTP isoform B. The data from this study will be presented.

Synthesis of phosphonate analogs of pyridoxamine as potential inhibitors of LMW-PTP

247th National Meeting (2014)

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