Designing protein–material interfaces
- Pacific Northwest National Laboratory (PNNL), Richland, WA (United States); Univ. of Washington, Seattle, WA (United States)
- Univ. of Washington, Seattle, WA (United States)
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 a class of designed helical repeat proteins that present a repeating pattern of charged amino acid residues. 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. Furthermore, 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. Moreover, the results demonstrate the vast potential of protein design in materials science and elucidate the mechanisms by which interactions between biomolecules and inorganic surfaces lead to unique materials and morphologies.
- Research Organization:
- Pacific Northwest National Laboratory (PNNL), Richland, WA (United States); Univ. of Washington, Seattle, WA (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- AC05-76RL01830; SC0019288
- OSTI ID:
- 3009076
- Alternate ID(s):
- OSTI ID: 3013706
- Report Number(s):
- PNNL-SA--212650
- Journal Information:
- MRS Bulletin, Journal Name: MRS Bulletin Vol. 50; ISSN 1938-1425; ISSN 0883-7694
- Publisher:
- Materials Research SocietyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
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