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

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 distinc...

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Bibliographic Details
Published in:Chemical communications (Cambridge, England) England), 2022-06, Vol.58 (49), p.6958-6961
Main Authors: Kakkis, Albert, Golub, Eyal, Choi, Tae Su, Tezcan, F. Akif
Format: Article
Language:English
Subjects:
Chemistry
Coordination compounds
Hydrophobic and Hydrophilic Interactions
Ligands
Metalloproteins - chemistry
Metals - chemistry
Oxidation-Reduction
Proteins
Self-assembly
Structural analysis
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Summary: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. 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.
ISSN:1359-7345
1364-548X
DOI:10.1039/d2cc02440c