Prediction of the interaction between HIV viruses and Human Serum Albumin (HSA) molecules using an equilibrium dynamics simulation program for application in bio medical science

A Karimipour and A Karimipour and NA Jolfaei and M Hekmatifar and D Toghraie and R Sabetvand and S Rostami, JOURNAL OF MOLECULAR LIQUIDS, 318, 113989 (2020).

DOI: 10.1016/j.molliq.2020.113989

Atomic interaction of Human Serum Albumin (HSA) protein and HIV virus is important in medical sciences. In the present study, for the first time, Molecular Dynamics (MD) simulation based on Newton's law used to predict the destruction of USA structure by the HN virus with atomic. In our research, each HSA and HIV molecules are simulated by As, C, Ca, Cl, N, O. and S atoms and contrived by DREIDING and Universal Force Fields to describe their atomic evolution. The atomic interaction between these structures described by calculating the total energy, center of mass distance, diffusion coefficient and volume of atomic structures. The calculated rates for these physical parameters show the attraction force between HSA protein and HIV virus, in which the COM distances of these structures varies from 7.7 A to 3.62 angstrom after 1 ns. Structurally, the volume of HSA protein raises from 152,241 angstrom(3) to 163,697 angstrom(3) after atomic interaction with the HIV virus which this atomic manner shows the protein destruction. Further, the simulation result show that the environmental parameters such as temperature is an important factor in HAS protein and HIV virus mutual interaction, by increasing the temperature of the atoms from 300 K to 350 K the attraction force between these structures increases and diffusion coefficient of HIV virus into HSA protein changes from 0.43 mu m(2)/s to 035 mu m(2)/s. (C) 2020 Elsevier B.V. All rights reserved.

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