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Browsing Biotechnology by Author "Abu-Hadid, M. M."

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    Study of Progesterone interaction with Human Serum Albumin: Spectroscopic approach
    (2011-01-17) Abu Teir, M. M.; Ghithan, J. H.; Darwish, S. M.; Abu-Hadid, M. M.
    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.
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    Study the interaction of hydrophobic vitamins (vitamin E and vitamin D) with HSA using Spectroscopic techniques
    (Quality Scientific Publishing, 2014-06-25) Abu Teir, M. M; Abu Awwad, I.; Abu-Hadid, M. M.; Darwish, S. M.
    The interaction of hydrophobic vitamins (vitamin E and vitamin D) with human serum albumin(HSA) at physiological (pH 6.9- 7.4) has been studied using UV-VIS spectrometer, and an FT-IR spectroscopy. The interaction of hydrophobic vitamins (vitamin E and vitamin D) with HSA has been investigated by using UV-absorption, and Fourier transforms infrared (FT-IR) spectroscopy. The binding constants of vitamin E and vitamin D have been determined by UV-absorption. The values of the binding constants are calculated at room temperature: (1.21×102M-1) and (6.8×101M-1) for vitamin E- HSA and vitamin D- HSA mixtures, respectively. FT-IR spectroscopy with Fourier self- deconvolution technique and second derivative resolution enhancement procedures were applied in the analysis of the amide I, amid II, and amid III regions to determine the protein secondary structure and hydrophobic vitamins binding mechanisms. All peaks positions in the three amide regions (amid I, amide II and amide III) have been assigned and any changes due to concentration changes have been investigated. The FTIR spectra measurements indicate a change in the intensity of absorption bands due to change in the concentrations in drugs. In addition a larger intensity decrease in the absorption band of α-helix relative to that of β-sheets has been observed. 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.