Issue 49, 2022

Redox- and metal-directed structural diversification in designed metalloprotein assemblies

Abstract

Herein we describe a designed protein building block whose self-assembly behaviour is dually gated by the redox state of disulphide bonds and the identity of exogenous metal ions. This protein construct is shown – through extensive structural and biophysical characterization – to access five distinct oligomeric states, exemplifying how the complex interplay between hydrophobic, metal–ligand, and reversible covalent interactions could be harnessed to obtain multiple, responsive protein architectures from a single building block.

Graphical abstract: Redox- and metal-directed structural diversification in designed metalloprotein assemblies

Supplementary files

Article information

Article type
Communication
Submitted
29 Apr 2022
Accepted
24 May 2022
First published
25 May 2022

Chem. Commun., 2022,58, 6958-6961

Author version available

Redox- and metal-directed structural diversification in designed metalloprotein assemblies

A. Kakkis, E. Golub, T. S. Choi and F. A. Tezcan, Chem. Commun., 2022, 58, 6958 DOI: 10.1039/D2CC02440C

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