title: Peptide-formation on cysteine-containing peptide scaffolds.
abstract: Monomeric cysteine residues attached to cysteine-containing peptides by disulfide bonds can be activated by carbonyldiimidazole. If two monomeric cysteine residues, attached to a 'scaffold' peptide Gly-Cys-Glyn-Cys-Glu10, (n = 0, 1, 2, 3) are activated, they react to form the dipeptide Cys-Cys. in 25-65% yield. Similarly, the activation of a cysteine residue attached to the 'scaffold' peptide Gly-Cys-Gly-Glu10 in the presence of Arg5 leads to the formation of Cys-Arg5 in 50% yield. The significance of these results for prebiotic chemistry is discussed.
authors.affiliation: Salk Institute for Biological Studies, San Diego, CA 92186-5800, USA.
authors.forename: B C
authors.initials: BC
authors.lastname: Chu
authors.forename: L E
authors.initials: LE
authors.lastname: Orgel
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine; D003545:Cysteine; D004220:Disulfides; D008956:Models, Chemical; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis*; D011485:Protein Binding
chemical_list: D004220:Disulfides; D010455:Peptides; D001120:Arginine; D003545:Cysteine