Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7585689 | Food Chemistry | 2018 | 34 Pages |
Abstract
The molecular nature of interactions between β-casein and p-coumaric acid was studied following exposure of their solutions to ultra-high temperature (UHT at 145â¯Â°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 UV-vis, 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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Jasmeet Kaur, Lita Katopo, Andrew Hung, John Ashton, Stefan Kasapis,