Study of Progesterone interaction with Human Serum Albumin: Spectroscopic approach
| dc.contributor.author | Abu Teir, M. M. | |
| dc.contributor.author | Ghithan, J. H. | |
| dc.contributor.author | Darwish, S. M. | |
| dc.contributor.author | Abu-Hadid, M. M. | |
| dc.date.accessioned | 2018-09-15T11:28:00Z | |
| dc.date.available | 2018-09-15T11:28:00Z | |
| dc.date.issued | 2011-01-17 | |
| dc.description.abstract | The interaction between progesterone and human serum albumin has been investigated. This interaction was studied by UV-absorption and fluorescence spectroscopy. From spectral analysis progesterone showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (K) is estimated 6.56×102 M-1 at 293 K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine HSA secondary structure and progesterone binding mechanisms. The observed spectral changes indicate the formation of H-bonding between progesterone and HSA molecules which can be related to the intensity decrease in the absorption band of α-helix relative to that of 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 | 2146-0108 | |
| dc.identifier.uri | https://dspace.alquds.edu/handle/20.500.12213/890 | |
| dc.language.iso | en_US | en_US |
| dc.subject | progesterone | en_US |
| dc.subject | amide I-III | en_US |
| dc.subject | binding mode | en_US |
| dc.subject | binding constant | en_US |
| dc.subject | protein secondary structure | en_US |
| dc.subject | Fourier transform IR | en_US |
| dc.subject | UV–spectroscopy | en_US |
| dc.subject | Flurosence spectroscopy | en_US |
| dc.title | Study of Progesterone interaction with Human Serum Albumin: Spectroscopic approach | en_US |
| dc.type | Article | en_US |