Interaction of Retinol with HSA using Spectroscopic Techniques

The interaction between retinol and HSA has been investigated using UV-absorption spectrophotometry, fluorescence spectroscopy and Fourier Transform Infrared (FT-IR) spectroscopy.UV-absorption spectrophotometry showed an increase in the absorption intensity with increasing the molecular ratios of retinol to HSA, it is found that the value of the binding constant is estimated to be1.7176×102 M-1. FTIR spectroscopy is used in the mid infrared region with Fourier self deconvolution, second derivative, difference spectra, peak picking and curve fitting were used to determine the effect of Retinol on the protein secondary structure in the amides I, II and Ill regions. Analysis of FTIR absorbance spectra is found that the intensity of the absorption bands increased with increasing the molecular ratios of retinol, however from the deconvoluted and curve fitted spectra found that the absorbance intensity for α-helix decreases relative to β-sheets, this decrease in intensity is related to the formation of H- bonding in the complex molecules

Comparative studies on the interactions between human serum albumin, bovine serum albumin and cholesterol: ftir and fluorescence spectroscopy

The interaction of the human serum albumin (HSA), bovine serum albumin (BSA) with cholesterol has been investigated. The basic binding interaction was studied by FTIR and fluorescence spectroscopy. From spectral analysis cholesterol showed a strong ability to quench the intrinsic fluorescence of HSA and BSA through a static quenching mechanism. The binding constant (k) between HSA and cholesterol is estimated to be K=2.14 × 103 M-1 at 293 K while between BSA and cholesterol is estimated to be K=.1.12 × 103 M-1 at the same temperature. FTIR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure and cholesterol binding mechanisms. The observed spectral changes indicate a higher percentage of H-bonding between cholesterol and -helix compared to the percentage of H-bonding to cholesterol and -sheets.This work is supported by the German Research Foundation DFG grant No. DR228/24-

AN INVESTIGATION OF THE PHASE BEHAVIOR OF AN AQUEOUS SYSTEM THAT CONTAINS A POLYAMPHOLYTE AND POLY(ETHYLENE GLYCOL)

The phase behavior of aqueous two-phase polymer system containing poly(ethylene glycol) and a synthetic polyampholyte in 0.1 N KCl was studied as a function of pH. The top phase was poly(ethylene glycol)-rich and the bottom phase was polyampholyte-rich. The binodal curve was found to move towards lower concentrations of polymers with increasing pH as a result of decreased solubility of the polyampholyte. Phase compositions were correlated using a model based on Flory- Huggins theory. Also, a model based on excluded volume theory was used to correlate the binodal curve