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Site-specific protein photochemical covalent attachment to carbon nanotube side walls and its electronic impact on single molecule function

Thomas, Suzanne K. ORCID:, Jamieson, W. David ORCID:, Gwyther, Rebecca E. A., Bowen, Benjamin J., Beachey, Adam, Worthy, Harley L., MacDonald, J. Emyr ORCID:, Elliott, Martin ORCID:, Castell, Oliver K. ORCID: and Jones, D. Dafydd ORCID: 2020. Site-specific protein photochemical covalent attachment to carbon nanotube side walls and its electronic impact on single molecule function. Bioconjugate Chemistry 31 (3) , pp. 584-594. 10.1021/acs.bioconjchem.9b00719

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Functional integration of proteins with carbon-based nanomaterials such as nanotubes holds great promise in emerging electronic and optoelectronic applications. Control over protein attachment poses a major challenge for consistent and useful device fabrication, especially when utilizing single/few molecule properties. Here, we exploit genetically encoded phenyl azide photochemistry to define the direct covalent attachment of four different proteins, including the fluorescent protein GFP and a β-lactamase binding protein (BBP), to carbon nanotube side walls. AFM showed that on attachment BBP could still recognize and bind additional protein components. Single molecule fluorescence revealed that on attachment to SWCNTs function was retained and there was feedback to GFP in terms of fluorescence intensity and improved resistance to photobleaching; GFP is fluorescent for much longer on attachment. The site of attachment proved important in terms of electronic impact on GFP function, with the attachment site furthest from the chromophore having the larger effect on fluorescence. Our approach provides a versatile and general method for generating intimate protein–CNT hybrid bioconjugates. It can be potentially applied to any protein of choice; the attachment position and thus interface characteristics with the CNT can easily be changed by simply placing the phenyl azide chemistry at different residues by gene mutagenesis. Thus, our approach will allow consistent construction and modulate functional coupling through changing the protein attachment position.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Advanced Research Computing @ Cardiff (ARCCA)
Physics and Astronomy
Publisher: American Chemical Society
ISSN: 1043-1802
Date of First Compliant Deposit: 11 February 2020
Date of Acceptance: 18 November 2019
Last Modified: 20 May 2024 17:22

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