Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
Autori
Radibratović, MilicaAl-Hanish, Ayah
Minić, Simeon L.
Radomirović, Mirjana Ž.
Milčić, Miloš K.
Stanić-Vučinić, Dragana
Ćirković-Veličković, Tanja
Članak u časopisu (Recenzirana verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.
Ključne reči:
Apo α-Lactalbumin / Epigallocatechin-3-gallate / Fluorescence quenching / Molecular dynamics simulation / Noncovalent interactions / Protein stabilityIzvor:
Food Chemistry, 2019, 278, 388-395Izdavač:
- Elsevier
Finansiranje / projekti:
- Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (RS-172024)
- FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (EU-810752)
Napomena:
- This is the peer-reviewed version of the following article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.
- Supplementary material: https://cherry.chem.bg.ac.rs/handle/123456789/4849
Povezane informacije:
- Verzija dokumenta
https://cherry.chem.bg.ac.rs/handle/123456789/3733 - Verzija dokumenta
https://doi.org/10.1016/j.foodchem.2018.11.038 - Referenca
https://cherry.chem.bg.ac.rs/handle/123456789/4849
DOI: 10.1016/j.foodchem.2018.11.038
ISSN: 0308-8146
PubMed: 30583389
WoS: 000453529300048
Scopus: 2-s2.0-85056756045
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Radibratović, Milica AU - Al-Hanish, Ayah AU - Minić, Simeon L. AU - Radomirović, Mirjana Ž. AU - Milčić, Miloš K. AU - Stanić-Vučinić, Dragana AU - Ćirković-Veličković, Tanja PY - 2019 UR - http://cherry.chem.bg.ac.rs/handle/123456789/4848 AB - α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form. PB - Elsevier T2 - Food Chemistry T1 - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study VL - 278 SP - 388 EP - 395 DO - 10.1016/j.foodchem.2018.11.038 ER -
@article{ author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja", year = "2019", abstract = "α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.", publisher = "Elsevier", journal = "Food Chemistry", title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study", volume = "278", pages = "388-395", doi = "10.1016/j.foodchem.2018.11.038" }
Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry Elsevier., 278, 388-395. https://doi.org/10.1016/j.foodchem.2018.11.038
Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry. 2019;278:388-395. doi:10.1016/j.foodchem.2018.11.038 .
Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395, https://doi.org/10.1016/j.foodchem.2018.11.038 . .