Analysis of Aspirin-Human Serum Albumin Complex Interaction Using Various Spectroscopic Methods
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The binding mechanism of aspirin with human serum albumin (HSA) was investigated by various spectroscopic techniques namely UV absorption, fluorescence spectroscopy and FTIR. Fluorescence data indicated that aspirin quenched the intrinsic fluorescence of HSA by static mechanism and hydrophobic interaction play the main reason in the aspirin binding. By using fluorescence and UV absorption, it was found that the binding constant of aspirin-HSA complex is in the order of 104 M-1. FTIR results confirmed that the analysis of the secondary structure of HSA was changed due to the interaction of aspirin and a significant shift of the wavenumber values through amid bands was obtained.