[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(shí)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.