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Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size.


ABSTRACT: Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired by soft matter where interactions between the components are controlled to yield the desired structure, we have developed a methodology to assemble networks of proteins of one species which we can decorate with another, whose coverage we can tune. Consequently, the interfaces between domains of each component can also be tuned, with potential applications for example in energy - or electron - transfer. Our model system of eGFP and mCherry with tuneable interactions reveals control over domain sizes in the resulting networks.

SUBMITTER: Rios de Anda I 

PROVIDER: S-EPMC8294043 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature

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Decorated networks of native proteins: nanomaterials with tunable mesoscopic domain size.

Ríos de Anda Ioatzin I   Coutable-Pennarun Angélique A   Brasnett Christopher C   Whitelam Stephen S   Seddon Annela A   Russo John J   Anderson J L Ross JLR   Royall C Patrick CP  

Soft matter 20210707 28


Natural and artificial proteins with designer properties and functionalities offer unparalleled opportunity for functional nanoarchitectures formed through self-assembly. However, to exploit this potential we need to design the system such that assembly results in desired architecture forms while avoiding denaturation and therefore retaining protein functionality. Here we address this challenge with a model system of fluorescent proteins. By manipulating self-assembly using techniques inspired b  ...[more]

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