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dc.contributor.authorDarwish, Saqer M.
dc.description.abstractThe 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.en_US
dc.description.sponsorshipThis work is supported by the German Research Foundation DFG grant No. DR228/24-2.en_US
dc.publisherWorld Scientificen_US
dc.subjectbinding constanten_US
dc.subjectprotein secondary structureen_US
dc.subjectFT-IR spectroscopyen_US
dc.titleSpectroscopic study of propofol binding to human serum albuminen_US

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  • Biophysics Research Laboratory [16]
    The biophysics lab has been established at Al-Quds University in 2005 with a generous fund from the DFG of the Federal Republic of Germany. The lab has supported several research students in the fields of physics and biology; several of whom are currently finishing their Doctorates degrees in Germany and the U.S. The research lab provides services to students and faculty members in the physics, biology, chemistry, and environmental science programs, in addition to an open cooperation with the college of medicine, pharmacy and the Nanotechnology center.

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