Epicatechin-induced conformational changes in β-lactoglobulin B monitored by FT-IR spectroscopy

SpringerPlus
Alessandro NucaraMarina Carbonaro

Abstract

The interaction between whey carrier protein β-lactoglobulin B and (-)-epicatechin, a major dietary flavonoid with a wide range of health-promoting biological activities, was investigated by Fourier transform infrared spectroscopy in physiological conditions. Amide I spectra of epicatechin - β-lactoglobulin complexes, in D2O buffer solutions, pD= 6.8, at molar ratios from 0.5:1 to 15:1, were measured by using a cell device specifically created. Changes in secondary structure elements at increasing epicatechin concentrations were quantified. Two different trends were observed for the intensities of β-sheet, random coil, and side chain contributions. At molar ratios ≤2 the β-exposed strand contributions (1625 cm(-1)) increased at the expence of the β-antiparallel sheet band (1637 cm(-1)). At molar ratios >2 the intensities of both β structures slightly decreased. The same behaviour was observed for the side chain contributions (band around 1610 ÷ 1620 cm(-1)). In addition, a conformational transition to a slightly opened structure, followed by aggregate formation at the highest molar ratios, were revealed. The results suggest that binding of epicatechin to β-lactoglobulin in physiological conditions occurs at the surface of the p...Continue Reading

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Citations

Apr 7, 2016·Biochimica Et Biophysica Acta·M CarbonaroF Stellato
Feb 26, 2015·Physical Chemistry Chemical Physics : PCCP·Adele De NinnoLeonetta Baldassarre
Jun 21, 2017·International Journal of Biological Macromolecules·Francesca CaporalettiAlessandro Nucara

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Methods Mentioned

BETA
Infrared spectroscopy
X-ray

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