Authors
Yuhui Wei, Daniel M Czajkowsky, Wei Zheng, Lin Li, Limin Zhou, Xiaoliang Chen, Xingfei Zhou, Lihua Wang, Jun Hu, Zhifeng Shao, Chunhai Fan, Bin Li, Qian Li
Published in
Small (Weinheim an der Bergstrasse, Germany). Pages e75184. Aug 18, 2026. Epub Aug 18, 2026.
Abstract
The formation of two-dimensional protein crystallites on solid surfaces is crucial in both natural biological processes and bottom-up nanofabrication. However, direct molecular-level insight into the dynamic evolution of epitaxial interfaces has remained challenging. Here, using in situ atomic force microscopy, we reveal the two-dimensional crystallization dynamics of streptavidin on muscovite mica with single-molecule resolution. We directly imaged the initial formation of multiple orientation domains during the crystallization process, a direct consequence of epitaxial matching to the three-fold symmetry of the mica lattice. This metastable poly-domain structure then evolves into a single-oriented crystallite through two coexisting classical ripening pathways, i. e. Ostwald ripening and Smoluchowski-type coalescence. The dominance of a single domain orientation arises from a competitive selection process during ripening, in which the initially largest domain ultimately consumes the neighboring domains of other orientations. Our work establishes a paradigm of domain coarsening in biomolecular epitaxy, providing a solid foundation for the rational design of functional bio-nano interfaces.
PMID:
42610663
Bibliographic data and abstract were imported from PubMed on 18 Aug 2026.
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