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Updated: Sep 20, 2025

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
The role of hydrolysis on the fibrillization of walnut protein: Self-assembly behavior, structural characteristics
Chang Li1, Rui Chen1, Jiangjuan Yuan1
1State Key Laboratory of Efficient Production of Forest Resources, Beijing Key Laboratory of Forest Processing and Safety, College of Biological Sciences and Technology, Beijing Forestry University, Beijing 100083, China.
Abstract:
This study comparatively investigated the effects of heating time (pH 2.0, 90 °C, 0-12 h) on the self-assembly behavior, structural characteristics of walnut protein fibrils (WPF) and walnut protein hydrolysate fibrils (WPHF). The results showed that the thioflavin T fluorescence in WPHF increased rapidly during the initial heating phase (0-2 h), suggesting that hydrolysis pretreatment promoted fibril formation. After heating for 12 h, WPHF exhibited higher surface hydrophobicity than WPF, with a red-shift in λmax from 343.2 to 345.0 nm, indicating enhanced intermolecular interactions within the fibrils. More flexible fibrils were observed in the WPHF. FiberAPP analysis showed that the periodicity of WPHF increased to 87 nm. These results offer valuable insights about the structural characteristics and formation mechanisms of walnut protein-based fibrils.
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