Mechanochemically Programmed, Oligomer‐Selective Amyloid Assembly via Axial Rotation
6 affiliations
- 1Department of Biotechnology and Bioinformatics Korea University Sejong Republic of Korea
- 2Interdisciplinary Graduate Program for Artificial Intelligence Smart Convergence Technology Korea University Sejong Republic of Korea
- 3Digital Healthcare Center Sejong Institute for Business and Technology (SIBT) Korea University Sejong Republic of Korea
- 4Department of Digital Healthcare Engineering Korea University Sejong Republic of Korea
- 5Department of Biomedical Engineering Yonsei University Wonju Republic of Korea
- 6Biomedical Research Center Korea University Guro Hospital Seoul Republic of Korea
Abstract
Amyloid oligomers have been widely implicated as primary cytotoxic intermediates; however, their selective and potentially scalable production remains challenging due to rapid fibril amplification. Here, we demonstrated that sustained axial rotation enables programmable mechanochemical control over amyloid pathway selection without the use of chemical additives. Using a thermal axial rotator, native monomeric hen egg‐white lysozyme was incubated at 60°C under quantitatively tunable rotational speeds, thereby creating RPM‐dependent hydrodynamic boundary conditions through centrifugal and wall‐associated mechanical inputs. A discrete RPM‐dependent transition emerged, delineating a low‐RPM fibril‐amplifying regime, an intermediate transition regime, and a high‐RPM oligomer‐enriched regime. At lower rotational speeds, aggregation followed a fibril‐amplifying pathway characterized by elevated β‐sheet content and elongated fibrillar morphologies. At higher rotational speeds, fibrillar growth was strongly attenuated and oligomer‐enriched assemblies predominated. Spectroscopic analyses and atomic force microscopy revealed that axial rotation redistributes the amyloid assembly landscape rather than simply suppressing aggregation. Functionally, the RPM‐defined assemblies exhibited kinetically distinct seeding behaviors and were associated with differential cellular response profiles in SH‐SY5Y neuroblastoma cells. These findings demonstrate axial rotation–mediated hydrodynamic boundary control as a scalable, chemical‐free strategy for reprogramming amyloid assembly pathways and producing oligomer‐rich assemblies for structural and functional studies.
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BibTeX
@article{roh2026mechanochemically,
title = {{Mechanochemically Programmed, Oligomer‐Selective Amyloid Assembly via Axial Rotation}},
author = {Seokbeom Roh and Eunji Song and Minwoo Bae and Da Yeon Cheong and Sechan Han and Taeha Lee and Dain Kang and Jae Eon Lee and Seung Pil Pack and Hyungbeen Lee and Insu Park and Gyudo Lee},
journal = {Small (Weinheim an Der Bergstrasse, Germany)},
year = {2026},
month = aug,
doi = {10.1002/smll.75467},
url = {https://doi.org/10.1002/smll.75467},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Mechanochemically Programmed, Oligomer‐Selective Amyloid Assembly via Axial Rotation
AU - Seokbeom Roh
AU - Eunji Song
AU - Minwoo Bae
AU - Da Yeon Cheong
AU - Sechan Han
AU - Taeha Lee
AU - Dain Kang
AU - Jae Eon Lee
AU - Seung Pil Pack
AU - Hyungbeen Lee
AU - Insu Park
AU - Gyudo Lee
PY - 2026
DA - 2026/08/25
JO - Small (Weinheim an Der Bergstrasse, Germany)
DO - 10.1002/smll.75467
UR - https://doi.org/10.1002/smll.75467
AB - Amyloid oligomers have been widely implicated as primary cytotoxic intermediates; however, their selective and potentially scalable production remains challenging due to rapid fibril amplification. Here, we demonstrated that sustained axial rotation enables programmable mechanochemical control over amyloid pathway selection without the use of chemical additives. Using a thermal axial rotator, native monomeric hen egg‐white lysozyme was incubated at 60°C under quantitatively tunable rotational speeds, thereby creating RPM‐dependent hydrodynamic boundary conditions through centrifugal and wall‐associated mechanical inputs. A discrete RPM‐dependent transition emerged, delineating a low‐RPM fibril‐amplifying regime, an intermediate transition regime, and a high‐RPM oligomer‐enriched regime. At lower rotational speeds, aggregation followed a fibril‐amplifying pathway characterized by elevated β‐sheet content and elongated fibrillar morphologies. At higher rotational speeds, fibrillar growth was strongly attenuated and oligomer‐enriched assemblies predominated. Spectroscopic analyses and atomic force microscopy revealed that axial rotation redistributes the amyloid assembly landscape rather than simply suppressing aggregation. Functionally, the RPM‐defined assemblies exhibited kinetically distinct seeding behaviors and were associated with differential cellular response profiles in SH‐SY5Y neuroblastoma cells. These findings demonstrate axial rotation–mediated hydrodynamic boundary control as a scalable, chemical‐free strategy for reprogramming amyloid assembly pathways and producing oligomer‐rich assemblies for structural and functional studies.
SN - 1613-6810
SN - 1613-6829
ER -