Analysis of Aspirin-Human Serum Albumin Complex Interaction Using Various Spectroscopic Methods
Date
2018-08-07
Authors
Alsamamra, Husain
Khalifa, Khloud
Darwish, Saqer
Abuteir, Musa
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Abstract
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.
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Keywords
aspirin , HSA , binding mode and FTIR spectroscopy