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Stabilization of apo α-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study

Authorized Users Only
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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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
Keywords:
Molecular dynamics simulation / Fluorescence quenching / Protein stability / Noncovalent interactions / Epigallocatechin-3-gallate / Apo α-lactalbumin
Source:
Food Chemistry, 2019, 278, 388-395
Publisher:
  • 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
[ Google Scholar ]
8
5
URI
https://cer.ihtm.bg.ac.rs/handle/123456789/3212
Collections
  • Radovi istraživača / Researchers' publications
Institution/Community
IHTM
TY  - 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 . .

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