Abstract
Chromium(III) complexes have been known to increase insulin absorption and decrease glucose levels in the blood, so Cr(III) complexes can be used as an antidiabetic supplement especially for people with diabetes type 2. The experimentally Cr(III) complexes proven to decrease glucose level, but the role mechanism of Cr(III) complexes in the body until now there is no explain in detail. In this research, the interaction of Cr(III) phenylalanine [Cr(phe)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) phenylalanine. This research performed by computational calculations Hartree-Fock with basis set 6-31G, the interaction with PTP used the Autodock Vina software. The results showed that [Cr(phe)3] interact with 5 amino acids of PTP, i.e Leu(13), Arg(18), Ser(94), Asp(129) and Tyr(131) with the interaction energy of -6,6 Kcal/mol. The results showed that the interaction Cr(III) phenylalanine with PTP indicate hydrogen bonding with bond leght from 1,8 Å to 2,9 Å.
Published Version
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