Combined spectroscopic, molecular docking and quantum mechanics study of β-casein and p-coumaric acid interactions following thermal treatment

Kaur, J, Katopo, L, Hung, A, Ashton, J and Kasapis, S 2018, 'Combined spectroscopic, molecular docking and quantum mechanics study of β-casein and p-coumaric acid interactions following thermal treatment', Food Chemistry, vol. 252, pp. 163-170.


Document type: Journal Article
Collection: Journal Articles

Title Combined spectroscopic, molecular docking and quantum mechanics study of β-casein and p-coumaric acid interactions following thermal treatment
Author(s) Kaur, J
Katopo, L
Hung, A
Ashton, J
Kasapis, S
Year 2018
Journal name Food Chemistry
Volume number 252
Start page 163
End page 170
Total pages 8
Publisher Elsevier BV
Abstract The molecular nature of interactions between ?-casein and p-coumaric acid was studied following exposure of their solutions to ultra-high temperature (UHT at 145 °C). Interactions were characterised by employing multi-spectroscopic methods, molecular docking and quantum mechanics calculations. FTIR demonstrates that the ligand lies in the vicinity of the protein, hence inverting the absorbance spectrum of the complex. This outcome changes the conformational characteristics of the protein leading to a flexible and open structure that accommodates the phenolic microconstituent. Results are supported by UVvis, CD and fluorescence quenching showing considerable shifts in spectra with complexation. Molecular docking indicates that there is at least a hydrogen bond between p-coumaric acid and the peptide backbone of isoleucine (Ile27). Quantum mechanics calculations further argue that changes in experimental observations are also due to a covalent interaction in the protein-phenolic adduct, which according to the best predicted binding pose involves the side chain of lysine 47.
Subject Food Chemistry and Molecular Gastronomy (excl. Wine)
Keyword(s) Molecular interactions
p-Coumaric acid
Thermal processing
?-Casein
DOI - identifier 10.1016/j.foodchem.2018.01.091
Copyright notice © 2018 Published by Elsevier Ltd.
ISSN 0308-8146
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