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Title | Spatiotemporal Landscape for the Sophisticated Transformation of Protein Assemblies Defined by Multiple Supramolecular Interactions. |
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Journal, issue, pages | ACS Nano, Vol. 17, Issue 15, Page 15001-15011, Year 2023 |
Publish date | Aug 8, 2023 |
Authors | Long Li / Zhen Li / Ziying Wang / Shuyu Chen / Rongying Liu / Xuyang Xu / Zhi Zhang / Linfei Ye / Yu Ding / Quan Luo / Sheng Cao / Lei Zhang / Anne Imberty / Guosong Chen / |
PubMed Abstract | Precise protein assemblies not only constitute a series of living machineries but also provide an advanced class of biomaterials. Previously, we developed the inducing ligand strategy to generate ...Precise protein assemblies not only constitute a series of living machineries but also provide an advanced class of biomaterials. Previously, we developed the inducing ligand strategy to generate various fixed protein assemblies, without the formation of noncovalent interactions between proteins. Here, we demonstrated that controlling the symmetry and number of supramolecular interactions introduced on protein surfaces could direct the formation of unspecific interactions between proteins and induce various nanoscale assemblies, including coiling nanowires, nanotubes, and nanosheets, without manipulation of the protein's native surfaces. More importantly, these nanoscale assemblies could spontaneously evolve into more ordered architectures, crystals. We further showed that the transformation from the introduced supramolecular interactions to the interactions formed between proteins was crucial for pathway selection and outcomes of evolution. These findings reveal a transformation mechanism of protein self-assembly that has not been exploited before and may provide an approach to generate complex and transformable biomacromolecular self-assemblies. |
External links | ACS Nano / PubMed:37459282 |
Methods | EM (helical sym.) |
Resolution | 16.4 Å |
Structure data | EMDB-34879: The nanotube of Ralstonia solanacearum lectin(RSL) induced by F3R |
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