Binding of maltose to Human Serum Albumin: A Multi-spectroscopic Approach and Molecular dynamic simulation

Human Serum Albumin is the most vital carrierprotein which is responsible for 80% ofblood pressure in blood plasma that is synthesized inthe liver and the main role in the transport and constituents ofthe circulatory system.This protein is a mono polypeptide chain with 585 residues.Maltose is present in most herbal and food product. In the present study the interaction between maltose and HSA were investigated in vitro under simulative physiological conditions (pH=7) using many approach such asFluorescence spectroscopy, UV−Vis absorption, Molecular dynamics simulations and Molecular docking. Fluorescence spectroscopy analysis showed thatquenching mechanism of HSA was dynamic. The result of UV−Vis absorption demonstrated that HSA has a maxima absorbance peak at 278 nm due to Trp and Tyr residues. Themaxima absorption was decreased with increasing the maltose concentration.The Far-UV CD data showed that the maltose induced a change in the proportion of secondary structure.Spectrofluorometric and docking study obviously showed that the binding between maltose and HSA was essentially driven by the non-covalent interaction consist of hydrophobic interactions.This binding has a negative value of the Gibbs free energy.

Keywords:

Human Serum Albumin , Fluorescence spectroscopy , UV−Vis absorption , Molecular dynamics simulations and Molecular docking