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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.

SUBMITTER: Kakkis A

PROVIDER: S-EPMC9419291 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature

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

Kakkis Albert A Golub Eyal E Choi Tae Su TS Tezcan F Akif FA

Chemical communications (Cambridge, England) 20220616 49

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 architectu ...[more]

PMID: 35642584

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