Structural Basis of Amyloid Fibril Assembly by Plant Seed Storage Proteins
Yiling Zhang, Danni Li, Qinyue Zhao, Shiran Lv, Wencheng Xia, Yongyi Xu, Yingshan Li, Yunxia Li, Yaoyang Zhang, Dan Li, Bo Sun, Wenyan Kang, Cong Liu, Bin Dai · 2026
Read Structural Basis of Amyloid Fibril Assembly by Plant Seed Storage Proteins by Yiling Zhang, Danni Li, Qinyue Zhao, Shiran Lv, Wencheng Xia, Yongyi Xu, Yingshan Li, Yunxia Li, Yaoyang Zhang, Dan Li, Bo Sun, Wenyan Kang, Cong Liu, Bin Dai (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/PMC13518808.txt.
Description
Yiling Zhang and colleagues examine in 2026 how plant seed storage proteins fold into amyloid fibrils, the tightly ordered protein fibers best known from brain disease. Animal amyloids have been mapped atom by atom, while plant versions stayed largely unexplored. The team tested oat 12S globulin, soybean 7S globulin, and rice glutelin under harsh cooking-like acidity and heat.
Oat and rice proteins formed fibrils both purified and inside whole-seed extracts, while soybean protein formed them only when purified. Cryo-electron microscopy revealed the oat fibril core at 3.9 angstrom resolution, a compact triangular shape held by dense hydrophobic and aromatic packing. Food scientists gain a structural starting point for plant-based amyloid materials.
Catalog record
| CREATOR | Yiling Zhang, Danni Li, Qinyue Zhao, Shiran Lv, Wencheng Xia, Yongyi Xu, Yingshan Li, Yunxia Li, Yaoyang Zhang, Dan Li, Bo Sun, Wenyan Kang, Cong Liu, Bin Dai |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 45 KB |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |