PMID- 30583389
OWN - NLM
STAT- MEDLINE
DCOM- 20190206
LR  - 20190215
IS  - 1873-7072 (Electronic)
IS  - 0308-8146 (Linking)
VI  - 278
DP  - 2019 Apr 25
TI  - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: 
      Experimental and molecular dynamics study.
PG  - 388-395
LID - S0308-8146(18)31976-9 [pii]
LID - 10.1016/j.foodchem.2018.11.038 [doi]
AB  - alpha-Lactalbumin (ALA) is a Ca(2+)-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 Ca(2+) removal decreased 
      conformational stability of ALA, because of the local destabilization of 
      Ca(2+)-binding region. EGCG binding to apoALA increases its stability by 
      reverting of conformation and stability of Ca(2+)-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 Ca(2+)-free form.
CI  - Copyright (c) 2018 Elsevier Ltd. All rights reserved.
FAU - Radibratovic, Milica
AU  - Radibratovic M
AD  - Center for Chemistry - Institute of Chemistry, Technology and Metallurgy, 
      University of Belgrade, Belgrade, Serbia.
FAU - Al-Hanish, Ayah
AU  - Al-Hanish A
AD  - Center of Excellence for Molecular Food Sciences & Department of Biochemistry, 
      University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
FAU - Minic, Simeon
AU  - Minic S
AD  - Center of Excellence for Molecular Food Sciences & Department of Biochemistry, 
      University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
FAU - Radomirovic, Mirjana
AU  - Radomirovic M
AD  - Center of Excellence for Molecular Food Sciences & Department of Biochemistry, 
      University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
FAU - Milcic, Milos
AU  - Milcic M
AD  - Center for Computational Chemistry and Bioinformatics & Department of Inorganic 
      Chemistry, University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
FAU - Stanic-Vucinic, Dragana
AU  - Stanic-Vucinic D
AD  - Center of Excellence for Molecular Food Sciences & Department of Biochemistry, 
      University of Belgrade - Faculty of Chemistry, Belgrade, Serbia.
FAU - Cirkovic Velickovic, Tanja
AU  - Cirkovic Velickovic T
AD  - Center of Excellence for Molecular Food Sciences & Department of Biochemistry, 
      University of Belgrade - Faculty of Chemistry, Belgrade, Serbia; Ghent University 
      Global Campus, Yeonsu-gu, Incheon, South Korea; Faculty of Bioscience 
      Engineering, Ghent University, Ghent, Belgium. Electronic address: 
      Tanja.Velickovic@ghent.ac.kr.
LA  - eng
PT  - Journal Article
DEP - 20181113
PL  - England
TA  - Food Chem
JT  - Food chemistry
JID - 7702639
RN  - 0 (Apoproteins)
RN  - 0 (apo-alpha-lactalbumin)
RN  - 8R1V1STN48 (Catechin)
RN  - 9013-90-5 (Lactalbumin)
RN  - BQM438CTEL (epigallocatechin gallate)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Animals
MH  - Apoproteins/*chemistry/metabolism
MH  - Binding Sites
MH  - Calcium/chemistry
MH  - Catechin/*analogs & derivatives/chemistry/metabolism
MH  - Hydrogen-Ion Concentration
MH  - Lactalbumin/*chemistry/metabolism
MH  - *Molecular Dynamics Simulation
MH  - Protein Binding
MH  - Protein Denaturation
MH  - Protein Stability
MH  - Protein Structure, Secondary
MH  - Spectrometry, Fluorescence
OTO - NOTNLM
OT  - Apo alpha-lactalbumin
OT  - Epigallocatechin-3-gallate
OT  - Fluorescence quenching
OT  - Molecular dynamics simulation
OT  - Noncovalent interactions
OT  - Protein stability
EDAT- 2018/12/26 06:00
MHDA- 2019/02/07 06:00
CRDT- 2018/12/26 06:00
PHST- 2018/08/01 00:00 [received]
PHST- 2018/11/01 00:00 [revised]
PHST- 2018/11/06 00:00 [accepted]
PHST- 2018/12/26 06:00 [entrez]
PHST- 2018/12/26 06:00 [pubmed]
PHST- 2019/02/07 06:00 [medline]
AID - S0308-8146(18)31976-9 [pii]
AID - 10.1016/j.foodchem.2018.11.038 [doi]
PST - ppublish
SO  - Food Chem. 2019 Apr 25;278:388-395. doi: 10.1016/j.foodchem.2018.11.038. Epub 
      2018 Nov 13.