Journal
FOOD CHEMISTRY
Volume 185, Issue -, Pages 309-317Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2015.04.001
Keywords
2S albumins; Binding affinity; Epigallocatechin-3-gallate; Fluorophore quenching; Molecular docking; Peanut; Polyphenol
Funding
- GA of the Ministry of Education, Science and Technological Development of the Republic of Serbia [172024]
- FP7 RegPot project FCUB-ERA GA [256716]
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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 physiologically active green tea catechin. (C) 2015 Elsevier Ltd. All rights reserved.
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