High-symmetry ill-fitting subunits in 3D form aggregates of all dimensions
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arXiv
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| Format: | Preprint |
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2026
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| _version_ | 1866914568487305216 |
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| author | Govorun, Elena N. Lenz, Martin |
| author_facet | Govorun, Elena N. Lenz, Martin |
| contents | 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. |
| format | Preprint |
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arxiv_https___arxiv_org_abs_2604_01109 |
| institution | arXiv |
| publishDate | 2026 |
| record_format | arxiv |
| spellingShingle | High-symmetry ill-fitting subunits in 3D form aggregates of all dimensions Govorun, Elena N. Lenz, Martin Soft Condensed Matter 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. |
| title | High-symmetry ill-fitting subunits in 3D form aggregates of all dimensions |
| topic | Soft Condensed Matter |
| url | https://arxiv.org/abs/2604.01109 |