Yang et al. (Yang, Wang, Du, & Chen, 2023) found that hydrophobic interactions can promote the formation of β-sheet structure and facilitate the protein fibrillization. The prolonged heating time also promotes the aggregation of protein protofibrils as well as small molecule peptides, leading to a decrease in their surface hydrophobicity.
了解详细信息:Yang et al. (Yang, Wang, Du, & Chen, 2023) found that hydrophobic interactions can promote the formation of β-sheet structure and facilitate the protein fibrillization. The prolonged heating time also promotes the aggregation of protein protofibrils as well as small molecule peptides, leading to a decrease in their surface hydrophobicity.
www.sciencedirect.com/science/article/pii/S026800…The protein is first hydrolyzed to produce fibril-forming peptides that are utilized for the fabrication of the fibrils instead of intact proteins during this process. However, recent studies have demonstrated that both protein monomers and peptides are the main components of protein fibrils (Wei & Huang, 2020b). In addition to the above ...
www.sciencedirect.com/science/article/pii/S092422…Proteins undergo acid hydrolysis at pH 2, and the resulting peptides are assembled into fibrils by hydrophobic interactions, electrostatic interactions, hydrogen bonds and π-π stacking under thermal treatment.
www.sciencedirect.com/science/article/pii/S026800…The first strategy is to modify the structure and function of protein fibrils by influencing fibrillization, such as through pretreatment, incubation conditions, nuclei induction, and ingredient interactions.
www.sciopen.com/article/10.26599/FSHW.2024.92…This research shows that protein fibrils can be made from different protein sources (whey protein of milk, soy protein, potato protein) by heating an acidic protein solution....
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We here report that peptide hydrolysis is the rate-determining step for fibrillation of β-lactoglobulin in whey protein isolate. We also explore the observation that β-lactoglobulin nanofibrils of distinct morphologies are obtained by simply …
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