title: Bis(2-sulfanylethyl)amido peptides enable native chemical ligation at proline and minimize deletion side-product formation.
abstract: Native chemical ligation of C-terminal peptidyl prolyl alkylthioesters with N-terminal cysteinyl peptides usually exhibits poor kinetic rates compared to other C-terminal amino acid residues. It is shown here that the reaction is accompanied by the formation of a deletion side product which is minimized by using a bis(2-sulfanylethyl)amido (SEA) thioester surrogate at a mildly acidic pH.
authors.affiliation: UMR CNRS 8161, Pasteur Institute of Lille , 59021 Lille, France.
authors.forename: Laurent
authors.initials: L
authors.lastname: Raibaut
authors.forename: Phillip
authors.initials: P
authors.lastname: Seeberger
authors.forename: Oleg
authors.initials: O
authors.lastname: Melnyk
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D003545:Cysteine / Q000737:chemistry*; D004952:Esters; D007700:Kinetics; D008026:Ligation; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D013438:Sulfhydryl Compounds
chemical_list: D000596:Amino Acids; D004952:Esters; D010455:Peptides; D013438:Sulfhydryl Compounds; D011392:Proline; D003545:Cysteine