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Interaction between Curcumin and β-Casein: Multi-Spectroscopic and Molecular Dynamics Simulation Methods.

Ruichen Zhao^1,2, Xiaoli Qin¹, Jinfeng Zhong^1,2

¹College of Food Science, Southwest University, Chongqing 400715, China.

Molecules (Basel, Switzerland)

|August 27, 2021

Summary

This summary is machine-generated.

Curcumin binds strongly to beta-casein (β-casein) primarily through electrostatic interactions, especially at acidic pH. This binding enhances curcumin

Keywords:

fluorescence quenching hydrophobic interaction molecular docking secondary structure content thermodynamic parameters

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Area of Science:

Biochemistry
Molecular interactions
Food science

Background:

Curcumin exhibits poor bioavailability due to low solubility and stability.
Beta-casein (β-casein) is a major milk protein with potential for complexation with hydrophobic molecules.
Understanding curcumin-β-casein interactions is crucial for developing effective delivery systems.

Purpose of the Study:

To investigate the effect of temperature and pH on the interaction between curcumin and β-casein.
To elucidate the binding mechanism and thermodynamic parameters of the curcumin-β-casein complex.
To assess the structural changes in β-casein upon complexation with curcumin.

Main Methods:

Fluorescence spectroscopy
UV-Visible spectroscopy
Molecular docking
Molecular dynamics simulation

Main Results:

Curcumin binds to β-casein mainly via electrostatic interactions, with stronger binding at acidic pH (pH 2.0) than neutral pH (pH 7.4).
Spectroscopic analysis indicated static quenching of β-casein's intrinsic fluorescence by curcumin.
Molecular simulations revealed lower binding energy for the β-casein-curcumin complex at pH 2.0 and 298 K, alongside a decrease in α-helix content and an increase in random coil in β-casein.

Conclusions:

Curcumin forms a stable complex with β-casein, predominantly through electrostatic forces.
The binding is influenced by pH and temperature, with optimal conditions favoring complex formation at lower pH.
These findings provide insights into enhancing curcumin's bioavailability through complexation with β-casein.