Molecular Docking Studies of Chromium(III) Picolinate with Protein Tyrosine Phosphatase

Molecular Docking Studies of Chromium(III) Picolinate with Protein Tyrosine Phosphatase Yuli Ambarwati1, Muhamad A. Martoprawiro2, Irma Mulyani2, Ismunandar2, Djulia Onggo2 1Inorganic Chemistry Division, Faculty of Mathematics and Natural Sciences, Universitas Lampung, Jalan Sumantri Brojonegoro No 01, Lampung 35141, Indonesia 2Inorganic and Physical Chemistry Division, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Jalan Ganesha 10, Bandung 40132, Indonesia ABSTRACT—Chromium(III) complexes was suggested as an essential nutrient that play a role in carbohydrate metabolism. Many studies in biological activity of Cr(III) complexes as an antidiabetic have been performed. Based on in vitro studies, the ability of some Cr(III) complexes to inhibit tyrosine phosphatase activity of insulin receptor was proposed as the chemical mechanism of Cr(III) in glucose metabolism. In this research, the interaction of Cr(III) picolinate [Cr(pic)3] with protein tyrosine phosphatase (PTP) was studied by molecular docking. The aims this study was to identify the active site of PTP that binding with those Cr(III) picolinate. This research used computational calculations, the method used was Hartree-Fock with basis set 6-31G, the interaction with PTP used the Autodck Vina software. The results showed that [Cr(pic)3] interact with 6 amino acids of PTP, i.e Leu13, Ile16, Ser47, Trp49, Asn50 and Tyr131 with the interaction energy of -7,0 Kcal/mol. The results showed that the interaction between Cr(III) picolinate with PTP indicate Van der Waals interaction. Keywords: Chromium(III) picolinate, PTP, Docking