title: Protein stapling via azide-alkyne ligation.
abstract: Here we demonstrate a methodology, termed protein stapling, for the introduction of covalent constraints into recombinant proteins. Using the azide-alkyne click reaction as the stapling chemistry, we have improved the thermostability of a model leucine zipper protein. Additionally, stapling the core of the small, globular protein G resulted in improved binding to its target, immunoglobulin G.
authors.affiliation: Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544, USA. ajlink@princeton.edu.
authors.forename: Diya M
authors.initials: DM
authors.lastname: Abdeljabbar
authors.forename: Frank J
authors.initials: FJ
authors.lastname: Piscotta
authors.forename: Siyan
authors.initials: S
authors.lastname: Zhang
authors.forename: A
authors.initials: A
authors.lastname: James Link
mesh_terms: D000480:Alkynes / Q000737:chemistry*; D000595:Amino Acid Sequence; D001386:Azides / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D007074:Immunoglobulin G / Q000378:metabolism; D016350:Leucine Zippers; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary
chemical_list: D000480:Alkynes; D001386:Azides; D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D007074:Immunoglobulin G