Spectroscopic investigations of pentobarbital interaction with human serum albumin
| dc.contributor.author | Darwish, Saqer M. | |
| dc.contributor.author | Abu sharkh, Sawsan E. | |
| dc.contributor.author | Abu Teir, Musa M. | |
| dc.contributor.author | Makharza, Sami A. | |
| dc.contributor.author | Abu-hadid, Mahmoud M. | |
| dc.date.accessioned | 2018-09-10T18:27:31Z | |
| dc.date.available | 2018-09-10T18:27:31Z | |
| dc.date.issued | 2010-01-29 | |
| dc.description.abstract | The interaction between pentobarbital and human serum albumin has been investigated. The basic binding interaction was studied by UV-absorption and fluorescence spectroscopy. From spectral analysis pentobarbital showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (k) is estimated at 1.812 104 M 1 at 293 K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and drug binding mechanisms. The observed spectral changes of HSA–pentobarbital complex indicate a larger intensity decrease in the absorption band of a-helix relative to that of b-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 a-helix and b-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 | 0022-2860 | |
| dc.identifier.uri | https://dspace.alquds.edu/handle/20.500.12213/889 | |
| dc.language.iso | en_US | en_US |
| dc.publisher | Elsevier | en_US |
| dc.subject | Pentobarbital | en_US |
| dc.subject | HSA | 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 investigations of pentobarbital interaction with human serum albumin | en_US |
| dc.type | Article | en_US |