The effect of aspirin-HSA complexation on the protein secondary structure

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Abstract

This study was designed to determine the secondary structure of human serum albumin (HSA) in the presence of aspirin in H 2 O and D 2 O solutions at physiological pH, using aspirin concentrations of 0.0001-5 mM with final protein concentration of 2% w/v. UV-vis spectra and Fourier transform infrared (FTIR) difference spectroscopy with its self-deconvolution, second derivative resolution enhancement, and curve-fitting procedures were applied to characterize the drug binding mode, the binding constant, and the protein secondary structure in the aspirin-HSA complexes. Spectroscopic evidence showed that no aspirin-protein interaction occurs at very low drug concentration (0.0001 mM), whereas at higher drug contents (0.001-0.1 mM) the aspirin anion binding (H-bonding) is mainly through the ε-amino NH 3 + group with overall binding constant of K = 1.4 × 10 4 M -1 . At high drug concentrations (1-5 mM), acetylation of Lys-199 was observed. Aspirin binding results in protein secondary structural changes from that of the α-helix 55% (free HSA) to 49%, β-sheet 22% (free HSA) to 31%, β-anti 12% (free HSA) to 4% and turn 11% (free HSA) to 16% in the aspirin-HSA complexes..Key words: aspirin, protein, drug, binding mode, binding constant secondary structure, FTIR spectroscopy.

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