Binding of Vitamin K1(Phylloquinone) to Human Serum Albumin(HSA):Spectroscopic studies
Date
2014-09-07
Authors
Abu Teir, Musa M
Hourani, Ola
Darwish, Saker M
Abu-hadid, Mahmoud M
Journal Title
Journal ISSN
Volume Title
Publisher
Dr.V.K.Sharma
Abstract
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.
Description
Keywords
Vitamin K1 , amide I-III , binding mode , binding constant , protein secondary structure , Fourier transform IR , UV–spectroscopy , Fluorescence spectroscopy