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[Adv. Mater. Interfaces] Understanding Biomolecular Crystallization on Amyloid-like Superhydrophobic Biointerface
作者:Qian Wu, Aiting Gao, Fei Tao, Peng Yang*
關(guān)鍵字:Protein/Peptide crystallization; Superhydrophobic surface; Biointerface; Surface concentration; Wetting/dewetting
論文來源:期刊
具體來源:Adv. Mater. Interfaces
發(fā)表時間:2018年

The crystallization of proteins and peptides at an interface is an important process in natural and synthetic systems. However, a comprehensive understanding about this process is extremely rare, and the screening on crystallization conditions guided by current knowledge is often empirical and requires laborious work. This report addresses a new crystallization pathway that a superhydrophobic proteinaceous platform to deliver a compatible biointerface can preferentially induce crystallization of proteins and peptides. Unlike conventional recognition that the depinning based on a Cassie model followed by a transition to Wenzel model governs the matter crystallization on superhydrophobic surface, we presented a different opinion that mere Wenzel model from the beginning could induce biomolecular crystallization on superhydrophobic biointerface through the concentration effect. The existence of protein-based biointerface behaves as a key to achieve high-quality protein crystals, as the replacement of the biointerface with a common silica-based superhydrophobic surface leads to poorly crystallized objects. Such “Like Crystallizes Like” route is further applied to crystallize amyloid peptides on this superhydrophobic biointerface.

Adv. Mater. Interfaces admi.201701065, in press.

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