Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut.

2S albumins of peanuts are seed storage proteins, highly homologous in structure and described as major elicitors of anaphylactic reactions to peanut (allergens Ara h 2 and Ara h 6). Epigallocatechin-3-gallate (EGCG) is the most biologically potent polyphenol of green tea. Non-covalent interactions of EGCG with proteins contribute to its diverse biological activities. Here we used the methods of circular dichroism, fluorescence quenching titration, isothermal titration calorimetry and computational chemistry to elucidate interactions of EGCG and 2S albumins. Similarity in structure and overall fold of 2S albumins yielded similar putative binding sites and similar binding modes with EGCG. Binding affinity determined for Ara h 2 was in the range described for complexes of EGCG and other dietary proteins. Binding of EGCG to 2S albumins affects protein conformation, by causing an α-helix to ß-structures transition in both proteins. 2S albumins of peanuts may be good carriers of physiologically active green tea catechin.

Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white.

Polyphenols, the potent plant secondary metabolites, have beneficial effects on human health, but the mechanism(s) by which these effects are exerted is not well understood. Here, we present the detailed analysis of the interactions between the major green tea catechin, epigallo-catechin 3-gallate (EGCG), and the major dietary protein and allergen, ovalbumin (OVA). We show that EGCG binds to the pocket that partly overlaps with the previously identified IgE-binding region in OVA, and that this interaction induces structural changes in the allergen. Moreover, our ex vivo studies reveal that OVA binds IgE and stimulates degranulation of basophils, and that its uptake by monocytes proceeds at a slower rate in the presence of EGCG. This study provides further evidence in support of the proposed mechanism by which EGCG interactions with the food allergens contribute to its diverse biological activities and may impair antigen uptake by antigen-presenting cells.

A comparative study of in vitro cytotoxic, antioxidant, and antimicrobial activity of Pt(II), Zn(II), Cu(II), and Co(III) complexes with N-heteroaromatic Schiff base (E)-2-[N'-(1-pyridin-2-yl-ethylidene)hydrazino]acetate.

In search for novel biologically active metal based compounds, an evaluation of in vitro cytotoxic, antioxidant, and antimicrobial activity of new Pt(II) complex and its Zn(II), Cu(II), and Co(III) analogues, with NNO tridentately coordinated N-heteroaromatic Schiff base ligand (E)-2-[N'-(1-pyridin-2-yl-ethylidene)hydrazino]acetate, was performed. Investigation of antioxidative properties showed that all of the compounds have strong radical scavenging potencies. The Zn(II) complex showed potent inhibition of DNA cleavage by hydroxyl radical. A cytotoxic action of investigated compounds was evaluated on cultures of human promyelocitic leukaemia (HL-60), human glioma (U251), rat glioma (C6), and mouse melanoma (B16) cell lines. It was shown that binuclear pentacoordinated Zn(II) complex possesses a strong dose-dependent cytotoxic activity, of the same order of magnitude as cisplatin on B16, C6, and U251 cells. Furthermore, Zn(II) complex causes oxidative stress-induced apoptotic death of HL-60 leukemic cells, associated with caspase activation, phosphatidylserine externalization, and DNA fragmentation.