.png){kind=icon}
.png){kind=icon}
Return
Designing protein–material interfaces
.png){kind=icon}
PRE
AI
DOI：10.1557/s43577-025-01008-4.png)
.png){kind=icon}
Original request for help.png){kind=icon}
Share.png){kind=icon}
Save
Abstract
En 中文
This article addresses recent advances in using de novo protein design to create coherent interfaces between proteins and inorganic materials, either through protein self-assembly on crystal lattices or through directed nucleation and growth of crystals by protein scaffolds. Inspired by natural protein–crystal interfaces, we focus on designed helical repeat proteins that present a repeating pattern of charged amino acid residues that epitaxially match a target inorganic crystal lattice. We describe the use of in situ imaging and spectroscopic methods to investigate both the assembly of these proteins and their ability to direct crystal nucleation and growth. The findings reveal the importance of surface charge, facet-specific binding, solvent organization, and, more generally, the balance of protein–substrate–solvent interactions in determining how organized protein–materials interfaces emerge. The results highlight the vast potential of protein design in materials science and inform our understanding of the mechanisms by which interactions between biomolecules and inorganic surfaces lead to unique materials and morphologies.
Journal
IF:
4.9
Papers:
5.3K
Citations:
9.5K