Liver Alcohol dehydrogenase (LADH) catalyzes reversible oxidation of primary and secondary alcohols to aldehyde using NADH+ as a coenzyme. The aim of the present study was to validate preexisting biophysical characterization of erythritol using simulation studies of protein-erythritol-water interaction in solution at the molecular level. Two molecular dynamics simulations of the protein ADH in solution at room temperature were carried out, one in the presence (about 0.77 M) and another in the absence of erythritol. The erythritol molecules were observed to cluster and move toward the protein, and expel water from the protein surface and ultimately form hydrogen bonds with protein. Besides, the coating by erythritol was noticed to reduce the conformational fluctuations of the protein compared to the erythritolfree system. Conclusively, at a moderate concentration of erythritol solution, erythritol molecules cluster in the protein region and interact with ADH via many H-bonds that prevent the protein folding, although the data shown in the present study are contrary probably due to providing a minimum solution from water with an osmolyte like erythritol with 10 ns simulation and subsequently studying the desired interaction with protein using above solution using 15 ns of simulation. Over findings provide new insights into further exploration of the studies pertaining to ADH activity in alcoholic liver diseases leading to lever Cirrhosis.