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

Albert Kakkis; Eyal Golub; Tae Su Choi; F. Akif Tezcan

doi:https://doi.org/10.1039/d2cc02440c

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

Albert Kakkis, Eyal Golub, Tae Su Choi, F. Akif Tezcan

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	6958-6961
Number of pages	4
Journal	Chemical Communications
Volume	58
Issue number	49
DOIs	https://doi.org/10.1039/d2cc02440c
State	Published - 16 Jun 2022
Externally published	Yes

All Science Journal Classification (ASJC) codes

Electronic, Optical and Magnetic Materials
General Chemistry
Ceramics and Composites
Metals and Alloys
Materials Chemistry
Surfaces, Coatings and Films
Catalysis

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https://doi.org/10.1039/d2cc02440c

Cite this

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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.",

author = "Albert Kakkis and Eyal Golub and Choi, {Tae Su} and Tezcan, {F. Akif}",

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AU - Kakkis, Albert

AU - Golub, Eyal

AU - Choi, Tae Su

AU - Tezcan, F. Akif

PY - 2022/6/16

Y1 - 2022/6/16

N2 - 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.

AB - 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.

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U2 - https://doi.org/10.1039/d2cc02440c

DO - https://doi.org/10.1039/d2cc02440c

M3 - مقالة

C2 - 35642584

SN - 1359-7345

VL - 58

SP - 6958

EP - 6961

JO - Chemical Communications

JF - Chemical Communications

IS - 49

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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