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- Title
Understanding Biomolecular Crystallization on Amyloid‐Like Superhydrophobic Biointerface.
- Authors
Wu, Qian; Gao, Aiting; Tao, Fei; Yang, Peng
- Abstract
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.
- Subjects
BIOLOGICAL interfaces; CRYSTALLIZATION; SUPERHYDROPHOBIC surfaces; BIOMOLECULAR electronics; CONTACT angle
- Publication
Advanced Materials Interfaces, 2018, Vol 5, Issue 6, p1
- ISSN
2196-7350
- Publication type
Article
- DOI
10.1002/admi.201701065