Protein 2D crystals possess diverse structures, and chemical and biological functions, due to the diversity of their protein building blocks. In nature, protein building blocks can self-assemble into 2D crystalline arrays on the templates of cell membrane or walls, like purple-membrane assembles and bacterial S-layer proteins, respectively, to realize specific biological functions. In the biomimetic filed, the current protocol for protein 2D crystals generally relay on lipid layers as supports. It is challenging to create protein 2D crystals with specific long-range order, due to the anisotropy of lipid template along its surface. That maybe the obstacle for the functional applications of protein 2D crystalline arrays in future.<br/>To address this issue, we used the variant of L-rhamnulose-1-phosphate aldolase (RhuA), <sup>C98</sup>RhuA, with incorporated Cys to self-assemble into 2D crystals on solid-liquid interface of mica. By carefully selecting cations and controlling their amounts on mica surface, we created different isotropic protein 2D crystals with diverse packing patterns along uniform direction. It inspires the novel strategy to synthesize protein 2D crystals at solid-liquid interface artificially. It also reminds us the importance of surface templating and entropy in the self-assembly of protein 2D structures both in nature and in human manner.

Surface templating and entropy-driven effect to the self-assembly of protein 2D crystal at solid-liquid interface

255th National Meeting (2018)

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