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
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