Alcohol-induced retarded protein dynamics of human serum albumin unveiled by temperature jump

The addition of ethanol at concentrations <= 1.0 vol% in human serum albumin (HSA) at the physiological concentration (ca. 47 mg L-1) does not influence the secondary structure but decelerates the protein dynamic process of HSA upon thermal stimulus probed by fluorescent temperature jump technique. The biological implication may be that inebriated persons are less sensitive to environmental stimuli because their HSA molecules may act more slowly when interacting with chemicals in the blood. This result provides an alternative perspective on the role of alcohol in perturbing the biological function of HSA at the molecular level.