Marth, Gabriella, Hartley, Andrew, Reddington, Samuel et al. (5 more authors) (2017) Precision templated bottom-up multiprotein nanoassembly through defined click chemistry linkage to DNA. ACS Nano. pp. 5003-5010. ISSN 1936-0851
Abstract
We demonstrate an approach that allows attachment of single-stranded DNA (ssDNA) to a defined residue in a protein of interest (POI) so as to provide optimal and well-defined multicomponent assemblies. Using an expanded genetic code system, azido-phenylalanine (azF) was incorporated at defined residue positions in each POI; copper-free click chemistry was used to attach exactly one ssDNA at precisely defined residues. By choosing an appropriate residue, ssDNA conjugation had minimal impact on protein function, even when attached close to active sites. The protein-ssDNA conjugates were used to (i) assemble double-stranded DNA systems with optimal communication (energy transfer) between normally separate groups and (ii) generate multicomponent systems on DNA origami tiles, including those with enhanced enzyme activity when bound to the tile. Our approach allows any potential protein to be simply engineered to attach ssDNA or related biomolecules, creating conjugates for designed and highly precise multiprotein nanoscale assembly with tailored functionality.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 American Chemical Society |
Keywords: | DNA nanotechnology,copper-free click chemistry,energy transfer,expanded genetic code,origami,precision assembly,protein engineering |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Electronic Engineering (York) |
Depositing User: | Pure (York) |
Date Deposited: | 20 Jul 2021 12:20 |
Last Modified: | 09 Dec 2024 00:10 |
Published Version: | https://doi.org/10.1021/acsnano.7b01711 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1021/acsnano.7b01711 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:176353 |