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Interaction Mechanism between α-Lactalbumin and Caffeic Acid: A Multispectroscopic and Molecular Docking Study
Nasser Abdulatif Al-Shabib1, Javed Masood Khan1, Abdulaziz M Al-Amri2
1College of Food and Agriculture Sciences, Department of Food and Nutrition, King Saud University, Riyadh 11451, Saudi Arabia.
Caffeic acid (CA) binds to alpha-lactalbumin (ALA) through hydrogen bonding, causing structural changes. This interaction is spontaneous and exothermic, offering insights for the dairy industry and food nutrition.
Area of Science:
- Food Science
- Biochemistry
- Protein Chemistry
Background:
- Caffeic acid (CA) is a prevalent phenolic acid in various food sources.
- Alpha-lactalbumin (ALA) is a major whey protein with significant nutritional value.
Purpose of the Study:
- To elucidate the interaction mechanism between caffeic acid (CA) and alpha-lactalbumin (ALA).
- To investigate the structural and conformational changes in ALA upon CA binding.
Main Methods:
- Spectroscopic techniques (UV-visible, fluorescence quenching)
- Computational methods (in silico studies)
- Circular dichroism (CD) spectroscopy
Main Results:
- Static quenching mode observed, indicating a spontaneous and exothermic binding process.
- Hydrogen bonding identified as the primary interaction force, with specific amino acid residues (Ser112, Lys108) involved.
- CA binding induced conformational changes in ALA, increasing its α-helical structure.
Conclusions:
- CA-ALA interaction is governed by hydrogen bonds and is thermodynamically favorable.
- Findings provide valuable information for understanding CA interactions with whey proteins in food processing.
- This research contributes to advancements in dairy processing and food nutrition security.
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