title: Protein-templated peptide ligation.
abstract: Molecular templates bind particular reactants, thereby increasing their effective concentrations and accelerating the corresponding reaction. This concept has been successfully applied to a number of chemical problems with a strong focus on nucleic acid templated reactions. We present the first protein-templated reaction that allows N-terminal linkage of two peptides. In the presence of a protein template, ligation reactions were accelerated by more than three orders of magnitude. The templated reaction is highly selective and proved its robustness in a protein-labeling reaction that was performed in crude cell lysate.
authors.affiliation: Chemical Genomics Centre of the Max Planck Society, Otto-Hahn-Strasse 15, 44227 Dortmund (Germany).
authors.forename: Nicolas
authors.initials: N
authors.lastname: Brauckhoff
authors.forename: Gernot
authors.initials: G
authors.lastname: Hahne
authors.forename: Johannes T-H
authors.initials: JT
authors.lastname: Yeh
authors.forename: Tom N
authors.initials: TN
authors.lastname: Grossmann
mesh_terms: D050882:CREB-Binding Protein / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D051788:Myeloid-Lymphoid Leukemia Protein / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs
chemical_list: D018840:HSP70 Heat-Shock Proteins; D010446:Peptide Fragments; D051788:Myeloid-Lymphoid Leukemia Protein; D050882:CREB-Binding Protein
keywords: bioorthogonal reactions; peptide ligation; protein modification; solid-phase peptide synthesis; templated reactions