(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.
(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.
(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.