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Updated: Feb 13, 2026

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives
Published on: February 7, 2017
Allosterically Activated Protein Self-Assembly for the Construction of Helical Microfilaments with Tunable Helicity
Miaomiao Xu1, Lianxiao Liu1, Qiang Yan1
1State Key Laboratory of Molecular Engineering of Polymers, Department of Macromolecular Engineering, Fudan University, Shanghai, 200433, China.
Abstract:
Protein allostery, a chemical-to-mechanical effect that can precisely regulate protein structure, exists in many proteins. Herein, we demonstrate that protein allostery can be used to drive self-assembly for the construction of tunable protein architectures. Calmodulin (CaM) was chosen as a model allosteric protein. Ca2+ -mediated contraction of CaM to a closed state can activate CaM and its ligand to self-assemble into a 1D protein helical microfilament. Conversely, relaxation of CaM to the open state can unwind and further dissociate the helical assemblies. Fine regulation of the protein conformation by tuning the external Ca2+ level allows us to obtain various protein helical nanostructures with tunable helicity. This study offers a new approach toward chemomechanically controlled protein self-assembly.
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