Understanding Biomolecular Crystallization on Amyloid‐Like Superhydrophobic Biointerface

Abstract 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. In this paper a new crystallization pathway that a superhydrophobic proteinaceous platform, to deliver a compatible biointerface, can preferentially induce crystallization of proteins and peptides are addressed. Unlike conventional recognition that the depinning based on a Cassie model followed by a transition to Wenzel model governs the matter of crystallization on superhydrophobic surface, a different opinion that mere Wenzel model from the beginning can induce biomolecular crystallization on superhydrophobic biointerface through the concentration effect is presented. 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.