Allosterically Activated Protein Self-Assembly for the Construction of Helical Microfilaments with Tunable Helicity

Angewandte Chemie
Miaomiao XuQiang Yan

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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Citations

Feb 2, 2021·Inorganic Chemistry·Bei WangWeisheng Liu
Jul 13, 2021·Organic & Biomolecular Chemistry·Di ShiYun-Bao Jiang
Mar 17, 2020·Accounts of Chemical Research·Chendi Gao, Guosong Chen
Aug 19, 2021·Chemical Reviews·Jie ZhuF Akif Tezcan

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