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Updated: Jun 29, 2025

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
Published on: August 2, 2012
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.
Abstract:
The mechanism of ethanol-induced fibrillation of β-lactoglobulin (β-lg) in the acidic aqueous solution upon heating was investigated using various techniques, mainly thioflavin T fluorescence, atomic force microscopy, nonreducing electrophoresis, mass spectrometry, Fourier transform infrared spectroscopy, and circular dichroism spectroscopy. The results showed that fibrillation occurred with a heating time increase, but high ethanol content slowed down the process. At a low ethanol volume fraction, peptides existed after heating for 2 h, with long and straight fibrils formed after 4-6 h, while at a high ethanol volume fraction, the proteins aggregated with very few peptides appeared at the early stage of heating, and short and curved fibrils formed after heating for 8 h. Ethanol weakened the hydrophobic interactions between proteins in the aqueous solution; therefore the latter could not completely balance the electrostatic repulsion, and thus suppressing the fibrillation process. It is believed that the fibrillation of β-lg in the acidic solution upon heating is mainly dominated by the polypeptide model; however, ethanol inhibited the hydrolysis of proteins, and the self-assembly mechanism changed to the monomer model.
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