Spectroscopic Investigations of pentobarbital interaction with human serum albumin
| dc.contributor.author | Swasan Abu Sharkh | |
| dc.date.accessioned | 2017-05-03T09:37:03Z | |
| dc.date.available | 2017-05-03T09:37:03Z | |
| dc.date.issued | 2010-08-02 | |
| dc.description.abstract | <p>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 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.</p> | en |
| dc.description.abstract | <p>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 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.</p> | ar |
| dc.identifier.uri | https://hdl.handle.net/20.500.11888/9595 | |
| dc.title | Spectroscopic Investigations of pentobarbital interaction with human serum albumin | en |
| dc.title | Spectroscopic Investigations of pentobarbital interaction with human serum albumin | ar |
| dc.type | Other |
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