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dc.contributor.authorAbu Teir, M. M.
dc.contributor.authorGhithan, J. H.
dc.contributor.authorDarwish, S. M.
dc.contributor.authorAbu-Hadid, M. M.
dc.date.accessioned2018-09-15T11:28:00Z
dc.date.available2018-09-15T11:28:00Z
dc.date.issued2011-01-17
dc.identifier.issn2146-0108
dc.identifier.urihttps://dspace.alquds.edu/handle/20.500.12213/890
dc.description.abstractThe 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.sponsorshipThis work is supported by the German Research Foundation DFG grant No. DR228/24-2en_US
dc.language.isoen_USen_US
dc.subjectprogesteroneen_US
dc.subjectamide I-IIIen_US
dc.subjectbinding modeen_US
dc.subjectbinding constanten_US
dc.subjectprotein secondary structureen_US
dc.subjectFourier transform IRen_US
dc.subjectUV–spectroscopyen_US
dc.subjectFlurosence spectroscopyen_US
dc.titleStudy of Progesterone interaction with Human Serum Albumin: Spectroscopic approachen_US
dc.typeArticleen_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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