Related Experiment Video
Updated: Jul 3, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
Published on: August 20, 2018
The mechanism of peptide composition-mediated polymorphism of gluten amyloid fibril aggregates: Structural
Yulin Feng1, Jie Ren1, Huijuan Zhang2
1Tobacco Research Institute of Chinese Academy of Agricultural Sciences, Qingdao 266101, China.
Abstract:
To investigate the protein polymorphisms of gluten amyloid fibrils and the associated molecular mechanisms, the structural characterization and morphological analysis of amyloid fibrils prepared with different ratio of glutenin and gliadin peptides were conducted. The thioflavin T fluorescence intensity and conversion rate of fibrils increased significantly by 121.5% and 24.6%, respectively, when the ratio of glutenin peptide to gliadin peptide reached 3:2. Meanwhile, long, rigid fibrils formed in this ratio with tight molecular structure, as evidenced by minimal inter-sheet (9.01 Å) and inter-strand (4.41 Å) distance. The short, curly fibrils tended to form at low percentages of glutenin or gliadin peptides. In addition, correlation analyses showed that the morphological characteristics of the fibrils were correlated with the density of the internal molecular structure influenced by hydrogen bonding, hydrophobic, and electrostatic interaction. These outcomes were expected to provide deep theoretical support for the extended functional applications of gluten amyloid fibrils.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
Protein Organization

