Spectroscopic study of propofol binding to human serum albumin
| dc.contributor.author | Darwish, Saqer M. | |
| dc.date.accessioned | 2018-08-26T09:55:31Z | |
| dc.date.available | 2018-08-26T09:55:31Z | |
| dc.date.issued | 2010-11-10 | |
| dc.description.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. | en_US |
| dc.description.sponsorship | This work is supported by the German Research Foundation DFG grant No. DR228/24-2. | en_US |
| dc.identifier.issn | 1793-7035 | |
| dc.identifier.uri | https://dspace.alquds.edu/handle/20.500.12213/782 | |
| dc.language.iso | en_US | en_US |
| dc.publisher | World Scientific | en_US |
| dc.subject | Propofol | en_US |
| dc.subject | binding constant | en_US |
| dc.subject | protein secondary structure | en_US |
| dc.subject | FT-IR spectroscopy | en_US |
| dc.title | Spectroscopic study of propofol binding to human serum albumin | en_US |
| dc.type | Article | en_US |