Protein tyrosine phosphatases (PTPs) are a group of enzymes that remove phosphate groups from phosphorylated tyrosine residues on proteins. PTPs are a common post-translational modifier for regulating cellular growth, proliferation, differentiation, and transformation through specific cellular signaling pathways. Specifically, low molecular weight protein tyrosine phosphatase (LMW-PTP) impacts processes such as embryonic development and tumor dispersion. Only recently LMW-PTP was found to be not only a negative regulator of cell proliferation, but also a positive growth modulator. The effects of LMW-PTP on various biological processes make it a target for a diverse set of small molecule inhibitors. A known natural product inhibitor of LMW-PTP is pyridoxal-5'-phosphate (PLP), which is the active form of vitamin B6. PLP displays tight binding to LMW-PTP, but is also a cofactor for many other enzymes, thus PLP lacks the specificity required to be an effective inhibitor. The scope of this research is to model inhibitors of LMW-PTP human isoform II based on the natural product PLP, specifically carboxylic acid derivatives of this structure, and synthesize and test the inhibitory effects of these compounds using a biological assay.

Synthesis of novel inhibitors for low molecular weight protein tyrosine phosphatase (LMW-PTP)

247th National Meeting (2014)

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