Stabilization of apo α-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
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2019
Authors
Radibratović, Milica
Al-Hanish, Ayah
Minić, Simeon

Radomirović, Mirjana

Milčić, Miloš

Stanić-Vučinić, Dragana

Ćirković Veličković, Tanja

Article (Published version)

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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 epigallocatechin-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
Keywords:
Molecular dynamics simulation / Fluorescence quenching / Protein stability / Noncovalent interactions / Epigallocatechin-3-gallate / Apo α-lactalbuminSource:
Food Chemistry, 2019, 278, 388-395Publisher:
- Elsevier
Funding / projects:
- Molecular properties and modifications of some respiratory and nutritional allergens (RS-172024)
- FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (EU-810752)
DOI: 10.1016/j.foodchem.2018.11.038
ISSN: 0308-8146
PubMed: 30583389
WoS: 000453529300048
Scopus: 2-s2.0-85056756045
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IHTMTY - JOUR AU - Radibratović, Milica AU - Al-Hanish, Ayah AU - Minić, Simeon AU - Radomirović, Mirjana AU - Milčić, Miloš AU - Stanić-Vučinić, Dragana AU - Ćirković Veličković, Tanja PY - 2019 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/3212 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 epigallocatechin-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 α-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 and Radomirović, Mirjana and Milčić, Miloš 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 epigallocatechin-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 α-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., Radomirović, M., Milčić, M., Stanić-Vučinić, D.,& Ćirković Veličković, T.. (2019). Stabilization of apo α-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 S, Radomirović M, Milčić M, Stanić-Vučinić D, Ćirković Veličković T. Stabilization of apo α-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, Radomirović, Mirjana, Milčić, Miloš, Stanić-Vučinić, Dragana, Ćirković Veličković, Tanja, "Stabilization of apo α-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 . .