Theoretical Investigation of Interaction of Sorbitol Molecules with Alcohol Dehydrogenase in Aqueous Solution Using Molecular Dynamics Simulation |
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Authors: | Homayoon Bahrami Mansour Zahedi Ali Akbar Moosavi-Movahedi Homa Azizian Massoud Amanlou |
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Institution: | (1) Department of Chemistry, Faculty of Sciences, Shahid Beheshti University G.C., Evin, 19839-63113 Tehran, Iran;(2) Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran;(3) Department of Medicinal Chemistry, Tehran University of Medicinal Sciences, Tehran, Iran |
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Abstract: | The nature of protein–sorbitol–water interaction in solution at the molecular level, has been investigated using molecular
dynamics simulations. In order to do this task, two molecular dynamics simulations of the protein ADH in solution at room
temperature have been carried out, one in the presence (about 0.9 M) and another in the absence of sorbitol. The results show
that the sorbitol molecules cluster and move toward the protein, and form hydrogen bonds with protein. Also, coating by sorbitol
reduces the conformational fluctuations of the protein compared to the sorbitol-free system. Thus, it is concluded that at
moderate concentration of sorbitol solution, sorbitol molecules interact with ADH via many H-bonds that prevent the protein
folding. In fact, at more concentrated sorbitol solution, water and sorbitol molecules accumulate around the protein surface
and form a continuous space-filling network to reduce the protein flexibility. Namely, in such solution, sorbitol molecules
can stabilize a misfolded state of ADH, and prevent the protein from folding to its native structure. |
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