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Last Updated: 2 years ago

Possible Interaction: Epigallocatechin Gallate and Serum Albumin, Human

Research Papers that Mention the Interaction

A small amount of PA decreased the distance, while a large amount increased the distance up to 5.4 Å. EGCg increased the inter-domain distance in HSA and HSA-PA up to 2.8 and 7.6 Å, respectively.
Dynamic light scattering (DLS) data revealed that both PA and EGCg increased HSA aggregation.
EGCg increased HSA aggregation more significantly and promoted formation of aggregates that were more heterogenous.
Moreover, EGCg decreased α-helix content in HSA and HSA-PA to the same level.
Biomolecules  •  2019  |  View Paper
Results indicated that the existence of ECG and EGCG would influence the binding of TF to HSA and can increase the free concentration of TF.
Journal of biomolecular structure & dynamics  •  2019  |  View Paper
Fluorescence quenching result and difference spectra of UV absorption revealed the formation of static complex between EGCG , DOX, or EPI and HSA.
The binding of EGCG with HSA was driven by both enthalpy and entropy while the binding of DOX or EPI was mainly entropy driven.
Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy  •  2019  |  View Paper
These results suggest the reversible covalent modification of EGCg via Schiff-base formation, and that the immobilization of EGCg to HSA , through the formation of a stable complex, prevented the polymerization and decomposition of EGCg in human serum.
This indicates that the galloyl moiety participated in the interaction of EGCg with HSA and that this interaction was of critical importance in preventing EGCg oxidation.
Bioscience, biotechnology, and biochemistry  •  2011  |  View Paper
Data obtained by fluorescence spectroscopy, CD, and FTIR experiments along with the docking studies suggest that EGCG binds to residues located in subdomains IIa and IIIa of HSA.
We observed a quenching of fluorescence of HSA in the presence of EGCG.
Proteins  •  2006  |  View Paper
EGCG selectively oxidized lysine residues at the EGCG-binding domains in HSA to generate an oxidatively deaminated product, aminoadipic semialdehyde.
When HSA was incubated with EGCG in the phosphate-buffered saline (pH 7.4) at 37°C, the protein carbonylation was associated with the formation of EGCG-derived products, such as the protein-bound EGCG, oxidized EGCG, and aminated EGCG.
PloS one  •  2016  |  View Paper