Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut
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Milčić, Miloš K.
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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 alpha-helix to beta-structures transition in both proteins. 2S albumins of peanuts may be good carriers of phys...iologically active green tea catechin.
Keywords:2S albumins / Binding affinity / Epigallocatechin-3-gallate / Fluorophore quenching / Molecular docking / Peanut / Polyphenol
Source:Food Chemistry, 2015, 185, 309-317
- Elsevier Sci Ltd, Oxford
- Molecular properties and modifications of some respiratory and nutritional allergens (RS-172024)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3355