Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut
Authorized Users Only
2015
Authors
Mihailović-Vesić, JelenaStambolić, Ivan
Apostolović, Danijela
Milčić, Miloš K.
Stanić-Vučinić, Dragana
Ćirković-Veličković, Tanja
Article (Published version)
Metadata
Show full item recordAbstract
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 / PolyphenolSource:
Food Chemistry, 2015, 185, 309-317Publisher:
- Elsevier Sci Ltd, Oxford
Funding / projects:
- Molecular properties and modifications of some respiratory and nutritional allergens (RS-MESTD-Basic Research (BR or ON)-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-FP7-256716)
Note:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3355
DOI: 10.1016/j.foodchem.2015.04.001
ISSN: 0308-8146
PubMed: 25952873
WoS: 000355027100040
Scopus: 2-s2.0-84955160095
Collections
Institution/Community
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Mihailović-Vesić, Jelena AU - Stambolić, Ivan AU - Apostolović, Danijela AU - Milčić, Miloš K. AU - Stanić-Vučinić, Dragana AU - Ćirković-Veličković, Tanja PY - 2015 UR - https://cherry.chem.bg.ac.rs/handle/123456789/1718 AB - 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. PB - Elsevier Sci Ltd, Oxford T2 - Food Chemistry T1 - Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut VL - 185 SP - 309 EP - 317 DO - 10.1016/j.foodchem.2015.04.001 ER -
@article{ author = "Mihailović-Vesić, Jelena and Stambolić, Ivan and Apostolović, Danijela and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja", year = "2015", abstract = "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.", publisher = "Elsevier Sci Ltd, Oxford", journal = "Food Chemistry", title = "Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut", volume = "185", pages = "309-317", doi = "10.1016/j.foodchem.2015.04.001" }
Mihailović-Vesić, J., Stambolić, I., Apostolović, D., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2015). Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut. in Food Chemistry Elsevier Sci Ltd, Oxford., 185, 309-317. https://doi.org/10.1016/j.foodchem.2015.04.001
Mihailović-Vesić J, Stambolić I, Apostolović D, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut. in Food Chemistry. 2015;185:309-317. doi:10.1016/j.foodchem.2015.04.001 .
Mihailović-Vesić, Jelena, Stambolić, Ivan, Apostolović, Danijela, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut" in Food Chemistry, 185 (2015):309-317, https://doi.org/10.1016/j.foodchem.2015.04.001 . .