Diverse protein assembly driven by metal and chelating amino acids with selectivity and tunability.

Abstract:

:Proteins are versatile natural building blocks with highly complex and multifunctional architectures, and self-assembled protein structures have been created by the introduction of covalent, noncovalent, or metal-coordination bonding. Here, we report the robust, selective, and reversible metal coordination properties of unnatural chelating amino acids as the sufficient and dominant driving force for diverse protein self-assembly. Bipyridine-alanine is genetically incorporated into a D3 homohexamer. Depending on the position of the unnatural amino acid, 1-directional, crystalline and noncrystalline 2-directional, combinatory, and hierarchical architectures are effectively created upon the addition of metal ions. The length and shape of the structures is tunable by altering conditions related to thermodynamics and kinetics of metal-coordination and subsequent reactions. The crystalline 1-directional and 2-directional biomaterials retain their native enzymatic activities with increased thermal stability, suggesting that introducing chelating ligands provides a specific chemical basis to synthesize diverse protein-based functional materials while retaining their native structures and functions.

journal_name

Nat Commun

journal_title

Nature communications

authors

Yang M,Song WJ

doi

10.1038/s41467-019-13491-w

subject

Has Abstract

pub_date

2019-12-05 00:00:00

pages

5545

issue

1

issn

2041-1723

pii

10.1038/s41467-019-13491-w

journal_volume

10

pub_type

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