Research on the interaction of mechanism between aspirin and human serum albumin / 中国药理学通报

ABSTRACT

Aim To study the fluorescence spectroscopy of human serum albumin(HSA)and the interaction of aspirin and HSA.Methods The quenching mechanism of the fluorescence of human serum albumin by aspirin was studied with the fluorescence.The interaction dissociation constants KD of human serum albumin and aspirin were determined at different temperatures according to double reciprocal Lineweaver-Burk plot and the main binding force was discussed by thermodynamic equations.The effect of aspirin on human serum albumin was also studied by synchronous fluorescence spectrometry.Results The quenching mechanism of aspirin to human serum albumin was static quenching.The interaction dissociation constants KD at 37℃,25℃ was 1.44?10-3 and 1.96?10-3 mol?L-1 respectively.The thermodynamic parameters of the reaction was-19.73 kJ?mol-1(?H),-16.21 kJ?mol-1(?G),-11.77 kJ?mol-1(?S).Conclusions The main binding force between aspirin and HSA was Van der Waals interaction.Aspirin binding on the human serum albumin could change the serum protein conformation.