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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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An ultra-stable gold-coordinated protein cage displaying reversible assembly
Ali D Malay1,2, Naoyuki Miyazaki3, Artur Biela4,5
1Heddle Initiative Research Unit, RIKEN, Saitama, Japan.
Nature
|May 10, 2019
Summary
Researchers created a novel, ultra-stable artificial protein cage using metal coordination. This inducible protein assembly, controlled by gold or mercury ions, offers new possibilities for supramolecular chemistry and biomaterials.
Area of Science:
- Biochemistry
- Materials Science
- Synthetic Biology
Background:
- Protein cages are vital in nature for functions like compartmentalization and cargo delivery.
- Designing controllable, inducible protein assemblies remains a significant challenge in synthetic biology.
Purpose of the Study:
- To engineer an ultra-stable artificial protein cage with metal-controlled assembly and disassembly.
- To explore novel supramolecular geometries and robust protein linking strategies.
Main Methods:
- Utilized cysteine-substituted protein rings and gold(I)-triphenylphosphine compounds for self-assembly.
- Employed cryo-electron microscopy to characterize the resulting supramolecular structures.
- Investigated the role of metal coordination (gold and mercury) in cage formation.
Main Results:
- Successfully generated monodisperse artificial protein cages exceeding 2 MDa, based on an unprecedented Archimedean snub cube geometry.
- Confirmed the cage structure is stabilized by 120 S-Au(I)-S linkages and exhibits two chiral forms.
- Demonstrated extreme chemical and thermal stability, with facile disassembly triggered by reducing agents.
Conclusions:
- Established a method for creating robust, higher-order protein structures through metal-coordinated assembly.
- Expanded the design possibilities for supramolecular assemblies with novel geometries.
- Showcased the potential of metal-responsive protein cages for advanced applications.
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