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Browsing Biotechnology by Subject "binding constant"

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    Binding of Vitamin K1(Phylloquinone) to Human Serum Albumin(HSA):Spectroscopic studies
    (Dr.V.K.Sharma, 2014-09-07) Abu Teir, Musa M; Hourani, Ola; Darwish, Saker M; Abu-hadid, Mahmoud M
    The interaction of hydrophobic vitamin (vitamin K1) 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 vitamin (vitamin K1) with HSA has been investigated by using UV-absorption, and Fourier transforms infrared (FT-IR) spectroscopy. The binding constant of vitamin K1 has been determined by UV-absorption. The value of the binding constant for vitamin K1 -HSA is calculated at room temperature 293 K and it was determined as 60 M����. 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 vitamin 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.
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    Spectroscopic approach of the interaction study of Ceftriaxone and human serum albumin
    (Academic Journals, 2013-12-10) Abu Teir, M. M.; Ghithan, J.; Abu-Taha, M. I.; Darwish, S. M.; Abu-hadid, M. M
    Under physiological conditions, interaction between ceftriaxone and human serum albumin was investigated by using fluorescence spectroscopy and ultra violet (UV) absorption spectrum. From spectral analysis, ceftriaxone showed a strong ability to quench the intrinsic fluorescence of human serum albumin (HSA) through a static quenching procedure. The binding constant (k) is estimated as K=1.02× 103 M-1 at 298 K. Fourier transform infrared spectroscopy (FT-IR) spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and drug binding mechanisms. The observed spectral changes indicated the formation of H-bonding between ceftriaxone and HSA molecules at higher percentage for -helix than for the -sheets.
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    Spectroscopic study of propofol binding to human serum albumin
    (World Scientific, 2010-11-10) Darwish, Saqer M.
    The interaction of propofol and human serum albumin (HSA) has been investigated by UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FT-IR) spectroscopy. Propofol has shown a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (k) is estimated at a low value of 2.55×103 M−1 at 293K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure in the amide regions I, II and III. The observed spectral changes of HSA-propofol 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.
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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.