High-symmetry ill-fitting subunits in 3D form aggregates of all dimensions
Abstract
Proteins can combine into functional elements in living cells or self-assemble into unwanted structures in a number of diseases. The resulting aggregates often display filamentous morphologies across a large range of protein shapes and molecular interactions. This has led to the suggestion that filament formation could be a generic outcome of the aggregation of geometrically complex, ill-fitting objects, although such a mechanism has not been demonstrated in three dimensions. To address this problem, we theoretically study the self-assembly of three-dimensional identical, ill-fitting deformable subunits mimicking globular proteins in solution. In our model, self-assembling subunits incur deformations that accumulate as the aggregate size increases and can eventually hamper further assembly. We analytically predict the ground state morphologies of the resulting aggregates as a function of the subunit adhesivity and elasticity by mapping their mechanics onto those of two incompatible, interconnected networks. We find that zero-dimensional clusters, three-dimensional bulks as well as symmetry-broken one-dimensional filaments and two-dimensional layers can all form depending on assembly parameters. Poorly compressible, moderately adhesive subunits favor filaments. These findings hint at a generic pathway to control self-assembly in three dimensions and suggests that such mechanisms could be investigated in more realistic protein models.
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BibTeX
@misc{govorun2026highsymmetry,
title = {{High-symmetry ill-fitting subunits in 3D form aggregates of all dimensions}},
author = {Elena N. Govorun and Martin Lenz},
howpublished = {HAL},
year = {2026},
month = oct,
doi = {10.48550/arxiv.2604.01109},
eprint = {2604.01109},
archivePrefix = {arXiv},
url = {https://hal.science/hal-05779497v1},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - UNPB
TI - High-symmetry ill-fitting subunits in 3D form aggregates of all dimensions
AU - Elena N. Govorun
AU - Martin Lenz
PY - 2026
DA - 2026/10/05
PB - HAL
DO - 10.48550/arxiv.2604.01109
UR - https://hal.science/hal-05779497v1
AB - Proteins can combine into functional elements in living cells or self-assemble into unwanted structures in a number of diseases. The resulting aggregates often display filamentous morphologies across a large range of protein shapes and molecular interactions. This has led to the suggestion that filament formation could be a generic outcome of the aggregation of geometrically complex, ill-fitting objects, although such a mechanism has not been demonstrated in three dimensions. To address this problem, we theoretically study the self-assembly of three-dimensional identical, ill-fitting deformable subunits mimicking globular proteins in solution. In our model, self-assembling subunits incur deformations that accumulate as the aggregate size increases and can eventually hamper further assembly. We analytically predict the ground state morphologies of the resulting aggregates as a function of the subunit adhesivity and elasticity by mapping their mechanics onto those of two incompatible, interconnected networks. We find that zero-dimensional clusters, three-dimensional bulks as well as symmetry-broken one-dimensional filaments and two-dimensional layers can all form depending on assembly parameters. Poorly compressible, moderately adhesive subunits favor filaments. These findings hint at a generic pathway to control self-assembly in three dimensions and suggests that such mechanisms could be investigated in more realistic protein models.
ER -