Protein-Mediated Colloidal Assembly
Abstract
Programmable colloidal assembly enables the creation of mesoscale materials in a bottom-up manner. Although DNA oligonucleotides have been used extensively as the programmable units in this paradigm, proteins, which exhibit more diverse modes of association and function, have not been widely used to direct colloidal assembly. Here we use protein–protein interactions to drive controlled aggregation of polystyrene microparticles, either through reversible coiled-coil interactions or through intermolecular isopeptide linkages. The sizes of the resulting aggregates are tunable and can be controlled by the concentration of immobilized surface proteins. Moreover, particles coated with different protein pairs undergo orthogonal assembly. We demonstrate that aggregates formed by association of coiled-coil proteins, in contrast to those linked by isopeptide bonds, are dispersed by treatment with chemical denaturants or soluble competing proteins. Finally, we show that protein–protein interactions can be used to assemble complex core–shell aggregates. This work illustrates a versatile strategy for engineering colloidal systems for use in materials science and biotechnology.
Additional Information
© 2017 American Chemical Society. Received: August 1, 2017; Published: September 12, 2017. We thank Trudy Padmore for technical assistance with particle conjugation and Andres Collazo for assistance with confocal microscopy. This work was supported by Defense Advanced Research Projects Agency Biological Robustness in Complex Settings Contract HR001-15-C-0093. M.O is supported by the Nakajima Foundation. B.S. is supported by NIH Training Grant 1T32GM112592 and by the Rosen Center for Bioengineering. Imaging was performed in the Biological Imaging Facility, with the support of the Caltech Beckman Institute and the Arnold and Mabel Beckman Foundation. Author Contributions: M.O and B.R.S. contributed equally to this work. The authors declare the absence of any competing financial interests.Attached Files
Accepted Version - nihms914383.pdf
Supplemental Material - ja7b07798_si_001.pdf
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Additional details
- PMCID
- PMC5672941
- Eprint ID
- 81405
- DOI
- 10.1021/jacs.7b07798
- Resolver ID
- CaltechAUTHORS:20170913-101124804
- HR001-15-C-0093
- Defense Advanced Research Projects Agency (DARPA)
- Nakajima Foundation
- 1T32GM112592
- NIH Predoctoral Fellowship
- Donna and Benjamin M. Rosen Bioengineering Center
- Caltech Beckman Institute
- Arnold and Mabel Beckman Foundation
- Created
-
2017-09-13Created from EPrint's datestamp field
- Updated
-
2022-03-22Created from EPrint's last_modified field
- Caltech groups
- Rosen Bioengineering Center