Spectroscopic study of propofol binding to human serum albumin
Darwish, Saqer M.
واصفات البياناتعرض سجل المادة الكامل
The interaction of propofol and human serum albumin (HSA) has been investigated by UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FT-IR) spectroscopy. Propofol has shown a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (k) is estimated at a low value of 2.55×103 M−1 at 293K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure in the amide regions I, II and III. The observed spectral changes of HSA-propofol complex indicate a larger intensity decrease in the absorption band of α-helix relative to that of β-sheets. This variation in intensity is related indirectly to the formation of H-bonding in the complex molecules, which accounts for the different intrinsic propensities of α-helix and β-sheets.