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.
Bibliographical noteFunding Information:
The authors would like to thank Nicholas Wood, Yushi Yang and Levke Ortlieb for providing the code for image analysis. The authors are grateful for very enriching discussions with Peter Schurtenberger and Bob Evans, and to Jennifer McManus for a critical reading of the manuscript. The work of IRdA and JR was funded by a Leverhulme Trust Philip Leverhulme Prize. IRdA was supported by a doctoral scholarship from CONACyT. JR acknowledges support from the European Research Council Grant DLV-75918. IRdA, AC-P and CPR gratefully acknowledge the ERC Grant agreement no. 617266 ‘‘NANOPRS’’ for financial support and Engineering and Physical Sciences Research Council (EP/H022333/1). The Ganesha X-ray scattering apparatus used for this research was purchased under EPSRC Grant ‘‘Atoms to Applications’’ (EP/K035746/1). This work benefitted from the SasView software, originally developed by the DANSE project under NSF award DMR-0520547.
© The Royal Society of Chemistry 2021.
- Bristol BioDesign Institute
- Synthetic biology