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Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles
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Emergent complexity from simple anisotropic building blocks: shells, tubes, and spirals.

Szilard N Fejer1, Dwaipayan Chakrabarti, David J Wales

  • 1University Chemical Laboratories, Lensfield Road, Cambridge CB2 1EW, United Kingdom.

ACS Nano
|January 9, 2010
PubMed
Summary
This summary is machine-generated.

A simple model with anisotropic interactions explains complex mesoscopic structure assembly. It reproduces diverse morphologies and matches experimental observations in capsid assembly.

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Area of Science:

  • Biophysics
  • Materials Science
  • Computational Modeling

Background:

  • Mesoscopic structures exhibit complex morphologies.
  • Understanding the physical principles governing self-assembly is crucial.
  • Existing models may not fully capture the diversity of observed structures.

Purpose of the Study:

  • To develop a simple, generic coarse-grained model for mesoscopic structure assembly.
  • To elucidate the physical principles driving the formation of complex morphologies.
  • To validate the model against experimental observations.

Main Methods:

  • Development of a coarse-grained model with anisotropic interactions.
  • Characterization of global minima for clusters across various parameters.
  • Simulation and analysis of structure formation.

Main Results:

  • The model successfully reproduces diverse global minima morphologies, including spheroidal shells, tubular, helical, and head-tail structures.
  • Anisotropic interactions are shown to be key drivers of specific morphology formation.
  • The model accurately captures experimental phenomena like competing morphologies and capsid polymorphism.

Conclusions:

  • A simple anisotropic interaction model provides a powerful framework for understanding mesoscopic self-assembly.
  • The model elucidates the physical basis for diverse complex structures observed in nature and experiments.
  • This approach offers insights into capsid assembly and the role of scaffolding proteins.