Show simple item record

dc.contributor.authorUrquhart, Taylor
dc.contributor.authorDaub, Elisabeth
dc.contributor.authorHonek, John 18:48:45 (GMT) 18:48:45 (GMT)
dc.descriptionThis document is the unedited Author’s version of a Submitted Work that was subsequently accepted for publication in Biconjugate Chemistry, copyright © American Chemical Society after peer review. To access the final edited and published work see
dc.description.abstractWith a mass of ~1.6 x 107 Daltons and com- posed of approximately 2700 proteins, bacteriophage M13 has been employed as a molecular scaffold in bionanomaterials fabrication. In order to extend the versatility of M13 in this area, residue-specific unnatural amino acid incorporation was employed to successfully display azide functionalities on specific solvent-exposed positions of the pVIII major sheath protein of this bacteriophage. Employing a combination of engineered mutants of the gene coding for the pVIII protein, the methionine (Met) analog, L-azidohomoalanine (Aha), and a suitable Escherichia coli Met auxotroph for phage pro- duction, conditions were developed to produce M13 bacteri- ophage labeled with over 350 active azides (estimated by fluorescent dye labeling utilizing a strain-promoted azide- alkyne cycloaddition) and capable of azide-selective attach- ment to 5 nm gold nanoparticles as visualized by transmis- sion electron microscopy. The capability of this system to undergo dual labeling utilizing both chemical acylation and bioorthogonal cycloaddition reactions was also verified. The above stratagem should prove particularly advantageous in the preparation of assemblies of larger and more complex molecular architectures based on the M13 building block.en
dc.description.sponsorshipNatural Sciences and Engineering Research Council University of Waterloo NSERC Canadian Graduate Scholarship (CGS-M) Ontario Graduate Scholarship Waterloo Institute for Nanotechnology Nanofellowshipen
dc.publisherAmerican Chemical Societyen
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International*
dc.titleBioorthogonal Modification of the Major Sheath Protein of Bacteriophage M13: Extending the Versatility of Bionanomaterial Scaffoldsen
dcterms.bibliographicCitationBioorthogonal Modification of the Major Sheath Protein of Bacteriophage M13: Extending the Versatility of Bionanomaterial Scaffolds Taylor Urquhart, Elisabeth Daub, and John Frank Honek Bioconjugate Chemistry Article ASAP DOI: 10.1021/acs.bioconjchem.6b00460en
uws.contributor.affiliation1Faculty of Scienceen

Files in this item


This item appears in the following Collection(s)

Show simple item record

Attribution-NonCommercial-NoDerivatives 4.0 International
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivatives 4.0 International


University of Waterloo Library
200 University Avenue West
Waterloo, Ontario, Canada N2L 3G1
519 888 4883

All items in UWSpace are protected by copyright, with all rights reserved.

DSpace software

Service outages