title: Superglue from bacteria: unbreakable bridges for protein nanotechnology.
abstract: Biotechnology is often limited by weak interactions. We suggest that an ideal interaction between proteins would be covalent, specific, require addition of only a peptide tag to the protein of interest, and form under a wide range of conditions. Here we summarize peptide tags that are able to form spontaneous amide bonds, based on harnessing reactions of adhesion proteins from the bacterium Streptococcus pyogenes. These include the irreversible peptide-protein interaction of SpyTag with SpyCatcher, as well as irreversible peptide-peptide interactions via SpyLigase. We describe existing applications, including polymerization to enhance cancer cell capture, assembly of living biomaterial, access to diverse protein shapes, and improved enzyme resilience. We also indicate future opportunities for resisting biological force and extending the scope of protein nanotechnology.
authors.affiliation: Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
authors.forename: Gianluca
authors.initials: G
authors.lastname: Veggiani
authors.affiliation: MIT Synthetic Biology Center, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
authors.forename: Bijan
authors.initials: B
authors.lastname: Zakeri
authors.affiliation: Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: mark.howarth@bioch.ox.ac.uk.
authors.forename: Mark
authors.initials: M
authors.lastname: Howarth
mesh_terms: D018829:Adhesins, Bacterial; D001709:Biotechnology; D008958:Models, Molecular; D036103:Nanotechnology; D015202:Protein Engineering; D011994:Recombinant Proteins; D013297:Streptococcus pyogenes
chemical_list: D018829:Adhesins, Bacterial; D011994:Recombinant Proteins
keywords: biomimetic; mechanobiology; nanobiotechnology; protein engineering; supramolecular assembly; synthetic biology