Spectroscopic study of propofol binding to human serum albumin
Date
2010-11-10
Authors
Darwish, Saqer M.
Journal Title
Journal ISSN
Volume Title
Publisher
World Scientific
Abstract
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.
Description
Keywords
Propofol , binding constant , protein secondary structure , FT-IR spectroscopy