title: Enhancing the efficiency of sortase-mediated ligations through nickel-peptide complex formation.
abstract: A modified sortase A recognition motif containing a masked Ni(2+)-binding peptide was employed to boost the efficiency of sortase-catalyzed ligation reactions. Deactivation of the Ni(2+)-binding peptide using a Ni(2+) additive improved reaction performance at low to equimolar ratios of the glycine amine nucleophile and sortase substrate. The success of this approach was demonstrated with both peptide and protein substrates.
authors.affiliation: Department of Chemistry, Western Washington University, 516 High Street, Bellingham, WA 98229, USA. john.antos@wwu.edu.
authors.forename: R
authors.initials: R
authors.lastname: David Row
authors.forename: Travis J
authors.initials: TJ
authors.lastname: Roark
authors.forename: Marina C
authors.initials: MC
authors.lastname: Philip
authors.forename: Lorena L
authors.initials: LL
authors.lastname: Perkins
authors.forename: John M
authors.initials: JM
authors.lastname: Antos
mesh_terms: D000595:Amino Acid Sequence; D019881:Aminoacyltransferases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D055162:Biocatalysis; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D007700:Kinetics; D009532:Nickel / Q000737:chemistry / Q000378:metabolism*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D010455:Peptides; D009532:Nickel; D019881:Aminoacyltransferases; C120542:sortase A; D003546:Cysteine Endopeptidases