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Controlling Solvent Polarity to Regulate Protein Self-Assembly Morphology and Its Universal Insight for Fibrillation
Bao Zhang1, Ruisheng Jiang1, Kexin Dong1
1Glyn O. Phillips Hydrocolloid Research Centre, National "111″ Center for Cellular Regulation and Molecular Pharmaceutics, Key Laboratory of Fermentation Engineering of Ministry of Education, Key Laboratory of Industrial Microbiology in Hubei Province, Department of Bioengineering and Food Science, Hubei University of Technology, Wuhan 430068, China.
Langmuir : the ACS Journal of Surfaces and Colloids
|March 28, 2024
Summary
Ethanol affects beta-lactoglobulin (β-lg) fibrillation during heating. High ethanol concentrations slow fibrillation, altering fibril structure and the underlying self-assembly mechanism from polypeptide to monomer models.
Area of Science:
- Biochemistry
- Protein Chemistry
- Materials Science
Background:
- Beta-lactoglobulin (β-lg) is a major whey protein.
- Protein fibrillation is implicated in various biological processes and diseases.
- Understanding fibrillation mechanisms is crucial for food science and biotechnology.
Purpose of the Study:
- To investigate the mechanism of ethanol-induced fibrillation of β-lg in acidic aqueous solution upon heating.
- To elucidate the role of ethanol concentration on the kinetics and morphology of β-lg fibrils.
- To determine how ethanol influences the self-assembly pathway of β-lg.
Main Methods:
- Thioflavin T fluorescence spectroscopy
- Atomic force microscopy (AFM)
- Nonreducing electrophoresis
- Mass spectrometry
- Fourier transform infrared (FTIR) spectroscopy
- Circular dichroism (CD) spectroscopy
Main Results:
- Fibrillation of β-lg increased with heating time, but was inhibited by high ethanol concentrations.
- Low ethanol concentrations led to long, straight fibrils after 4-6 h, while high concentrations resulted in short, curved fibrils after 8 h.
- Ethanol weakened hydrophobic interactions, suppressed electrostatic repulsion, and shifted the fibrillation mechanism from polypeptide to monomer models.
Conclusions:
- Ethanol significantly modulates the fibrillation process of β-lg.
- The concentration of ethanol dictates the rate, structure, and self-assembly mechanism of β-lg fibrils.
- Findings provide insights into protein aggregation control in the presence of organic solvents.
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