AI Article Synopsis
- The study examined how different metal ions (Cu, Sn, Zn, Mn, Al, Fe) affect the interaction between (-)-epigallocatechin-3-gallate (EGCg) and β-lactoglobulin (β-Lg) using fluorescence and circular dichroism (CD) spectroscopy.
- The presence of Cu significantly enhances the binding efficiency between EGCg and β-Lg, while Mn, Al, and Zn reduce it; specifically, Cu increases binding affinity by 115.44%, while the others show substantial decreases.
- CD spectroscopy revealed that both Cu and Al lead to a decrease in the α-helix content of β-Lg, indicating that these interactions cause structural changes in the protein.
Article Abstract
The effects of metal ions (Cu, Sn, Zn, Mn, Al and Fe) on the interaction between (-)-epigallocatechin-3-gallate (EGCg) and β-lactoglobulin (β-Lg) were investigated via fluorescence and circular dichroism (CD) spectroscopy. The results of the fluorescence titration experiment demonstrated that the addition of Cu increases the quenching efficiency of EGCg to β-Lg by more than EGCg alone, while Mn, Al and Zn decrease the quenching efficiency of EGCg to β-Lg by less than EGCg alone. [β-Lg-Mn], [β-Lg-Al], [β-Lg-Zn] and [β-Lg-Sn] obviously decreased the apparent binding affinities (K) of EGCg to β-Lg by 95.53%, 81.94%, 44.66% and 38.58%, respectively, whereas [β-Lg-Cu] significantly increased the K of EGCg for β-Lg by 115.44%. The results of CD spectroscopy experiment showed the α-helix content of β-Lg decreased with the addition of Cu or Al, indicating that the β-Lg-Cu and β-Lg-Al interaction resulted in unfolding of the secondary structure of β-Lg.
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| http://dx.doi.org/10.1016/j.foodchem.2016.11.158 | DOI Listing |
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