chimeric design, synthesis, and biological assays of a new nonpeptide insulin-mimetic vanadium compound to inhibit protein tyrosine phosphatase 1B

Prior to its total synthesis, a new vanadium coordination compound, called TSAG0101, was computationally designed to inhibit the enzyme protein tyrosine phosphatase 1B (PTP1B). The PTP1B acts as a negative regulator of insulin signaling by blocking the active site where phosphate hydrolysis of the insulin receptor takes place. TSAG001, (V V O 2 (OH)(picolinamide)), was characterized by infrared (IR) and nuclear magnetic resonance (NMR) spectroscopy; IR: ν/cm −1 3,570 (NH), 1,627 (C=O, coordinated), 1,417 (C−N), 970/842 (O=V=O), 727 δ . (pyridine ring); 13 C NMR: 5 bands between 122 and 151 ppm and carbonyl C shifted to 180