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Peer-reviewedCC BY 4.0Advanced Science

Hydrodynamic Selection of Polymorphic Assembly Pathways in Plant Protein Amyloid Fibrils

  • Zejian Xu1,2
  • Pengfei Yang1,2
  • Meng Li1,2
  • Zichen Cao1,2
  • Tian Lan1,2
  • Yan Zhang3
  • Weibiao Zhou4
  • Lianzhou Jiang1,2
  • Xiaonan Sui1,2
4 affiliations
  1. 1College of Food Science Northeast Agricultural University Harbin People's Republic of China
  2. 2Heilongjiang Joint Laboratory of Plant‐Based Food Science (International Cooperation) Harbin People's Republic of China
  3. 3College of Horticulture and Landscape Architecture Northeast Agricultural University Harbin People's Republic of China
  4. 4Department of Food Science and Technology National University of Singapore Singapore Singapore
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Abstract

Plant protein amyloid fibrils are universally assembled in liquid environments, yet their formation is often analyzed without explicitly considering the role of fluid motion. In practice, as a typical model system, soy protein amyloid fibrils (SAFs) are generated under dynamic hydrodynamic conditions involving shear and vortex transport. How such flow fields regulate fibril growth pathways and give rise to polymorphic assembly remains largely unexplored. Here, we elucidate the hydrodynamic selection of SAFs assembly pathways through nanoscale structural characterization combined with flow‐field analysis. Atomic force microscopy (AFM) identifies six distinct fibril morphologies, including short‐curved, javelin‐like, loop‐like, twisted ribbon, helical ribbon, and rod‐like structures. By integrating AFM observations with particle image velocimetry (PIV) results, we propose a drafting, kissing, and docking (DKD) dynamic as a plausible hydrodynamic model for understanding polymorphic fibril assembly. Computational fluid dynamics (CFD) simulations further reproduce key characteristics of the experimentally observed flow fields and provide hydrodynamic support for the proposed interpretation of fibrillation pathways. These results demonstrate that an in‐depth understanding of hydrodynamic selection behavior in polymorphic assembly pathways is important to pave the way for production of tailormade amyloid materials.

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Cite

BibTeXRIS
BibTeX
@article{xu2026hydrodynamic,
  title = {{Hydrodynamic Selection of Polymorphic Assembly Pathways in Plant Protein Amyloid Fibrils}},
  author = {Zejian Xu and Pengfei Yang and Meng Li and Zichen Cao and Tian Lan and Yan Zhang and Weibiao Zhou and Lianzhou Jiang and Xiaonan Sui},
  journal = {Advanced Science},
  year = {2026},
  month = oct,
  doi = {10.1002/advs.78458},
  url = {https://doi.org/10.1002/advs.78458},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Hydrodynamic Selection of Polymorphic Assembly Pathways in Plant Protein Amyloid Fibrils
AU  - Zejian Xu
AU  - Pengfei Yang
AU  - Meng Li
AU  - Zichen Cao
AU  - Tian Lan
AU  - Yan Zhang
AU  - Weibiao Zhou
AU  - Lianzhou Jiang
AU  - Xiaonan Sui
PY  - 2026
DA  - 2026/10/26
JO  - Advanced Science
DO  - 10.1002/advs.78458
UR  - https://doi.org/10.1002/advs.78458
AB  - Plant protein amyloid fibrils are universally assembled in liquid environments, yet their formation is often analyzed without explicitly considering the role of fluid motion. In practice, as a typical model system, soy protein amyloid fibrils (SAFs) are generated under dynamic hydrodynamic conditions involving shear and vortex transport. How such flow fields regulate fibril growth pathways and give rise to polymorphic assembly remains largely unexplored. Here, we elucidate the hydrodynamic selection of SAFs assembly pathways through nanoscale structural characterization combined with flow‐field analysis. Atomic force microscopy (AFM) identifies six distinct fibril morphologies, including short‐curved, javelin‐like, loop‐like, twisted ribbon, helical ribbon, and rod‐like structures. By integrating AFM observations with particle image velocimetry (PIV) results, we propose a drafting, kissing, and docking (DKD) dynamic as a plausible hydrodynamic model for understanding polymorphic fibril assembly. Computational fluid dynamics (CFD) simulations further reproduce key characteristics of the experimentally observed flow fields and provide hydrodynamic support for the proposed interpretation of fibrillation pathways. These results demonstrate that an in‐depth understanding of hydrodynamic selection behavior in polymorphic assembly pathways is important to pave the way for production of tailormade amyloid materials.
SN  - 2198-3844
ER  -