Related Experiment Video
Updated: May 9, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Formation of tiger nut protein fibrils through self-assembly and different nuclei-induced pathways: Focus on
Xinyu Jiang1, Yongliang Ma1, Feng Gao1
1College of Food Science and Engineering, Jilin University, Changchun 130062, PR China.
Abstract:
Tiger nut protein fibrils (TNPFs) were prepared through three pathways: self-assembly (TNPF), Homogeneous nuclei (HN)-induced (HN-TNPF), and Secondary nuclei (SN)-induced (SN-TNPF). Differences in morphology, structure, and formation mechanisms among the three TNPFs were examined. HN and SN, serving as fibrillation seeds, enhanced both fibril production and fibrillation rate. Compared to TNPF, the addition of HN and SN shortening the lag time from 3 (TNPF) to 2.2 (HN-TNPF) and 1.89 h (SN-TNPF), respectively. All three TNPFs exhibited fibril structures, notably, SN-TNPF displayed bifurcations on the trunk. Regarding secondary structure, a transition from α-helix to β-sheet was observed in all samples. The dynamic evolution of tertiary structure demonstrated that fibrillation was driven by non-covalent interactions and disulfide bond. After hydrolysis, the identification of specific peptides by LC-MS/MS and core region prediction using AMYLPRED2 showed 89.29 %, 82.22 %, and 89.74 % of peptide sequences in TNPF, HN-TNPF, and SN-TNPF, respectively, possessed fibril forming potential.
Related Concept Videos
Protein Folding
Protein Organization
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Fibrous Proteins
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...

