The State Key Laboratory of Molecular Engineering of Polymers and Department of Macromolecular Science, Fudan University, Shanghai 200433, China.
State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai 200438, China.
ACS Nano. 2023 Aug 8;17(15):15001-15011. doi: 10.1021/acsnano.3c04029. Epub 2023 Jul 17.
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.
精确的蛋白质组装不仅构成了一系列生命机器，而且还提供了一类先进的生物材料。在此之前，我们开发了诱导配体策略来产生各种固定的蛋白质组装，而无需在蛋白质之间形成非共价相互作用。在这里，我们证明了控制蛋白质表面上引入的超分子相互作用的对称性和数量可以指导蛋白质之间的非特异性相互作用的形成，并诱导各种纳米级组装，包括螺旋纳米线、纳米管和纳米片，而无需对蛋白质的天然表面进行操作。更重要的是，这些纳米级组装可以自发地演变成更有序的结构，即晶体。我们进一步表明，从引入的超分子相互作用到蛋白质之间形成的相互作用的转变对于途径选择和进化结果至关重要。这些发现揭示了以前未被利用的蛋白质自组装的转变机制，可能为生成复杂和可转换的生物大分子自组装提供了一种方法。
