Chemically Controlled Self-Assembly of Protein Nanorings
Abstract
The exploitation of biological macromolecules, such as nucleic acids, for the fabrication of advanced materials is a promising area of research. Although a greater variety of structural and functional uses can be envisioned for protein-based materials, systematic approaches for their construction have yet to emerge. Consistent with theoretical models of polymer macrocyclization, we have demonstrated that, in the presence of dimeric methotrexate (bisMTX), wild-type Escherichia coli dihydrofolate reductase (DHFR) molecules tethered together by a flexible peptide linker (ecDHFR2) are capable of spontaneously forming highly stable cyclic structures with diameters ranging from 8 to 20 nm. The nanoring size is dependent on the length and composition of the peptide linker, on the affinity and conformational state of the dimerizer, and on induced protein−protein interactions. Delineation of these and other rules for the control of protein oligomer assembly by chemical induction provides an avenue to the future design of protein-based materials and nanostructures.
Additional Information
© 2006 American Chemical Society. Received 4 February 2006. Published online 17 May 2006. Published in issue 1 June 2006. We would like to thank the Division of Medicinal Chemistry−American Chemical Society for a Pre-doctoral Fellowship to J.C.T.C. This research was supported by a Ziagen Faculty Development Grant (C.R.W.) from the University of Minnesota, Department of Medicinal Chemistry, and an AHC Seed-grant (C.R.W.) from the University of Minnesota Academic Health Center. We would also like to thank Dr. Trevor Douglas for access to the electron microscopy facilities at Montana State University.Attached Files
Supplemental Material - ja060631e_si_001.pdf
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Additional details
- Eprint ID
- 114037
- DOI
- 10.1021/ja060631e
- Resolver ID
- CaltechAUTHORS:20220323-565490000
- American Chemical Society Division of Medicinal Chemistry
- University of Minnesota
- Created
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2022-03-25Created from EPrint's datestamp field
- Updated
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2022-03-25Created from EPrint's last_modified field