title: Peptide ligations accelerated by N-terminal aspartate and glutamate residues.
abstract: A novel application of intramolecular base catalysis confers enhanced reaction rates for aminolysis ligations between peptide thioesters and peptides bearing N-terminal aspartate or glutamate residues. The broad scope of this process and its application in the total synthesis of the diabetes drug exenatide is demonstrated.
authors.affiliation: School of Chemistry, The University of Sydney, NSW 2006, Australia.
authors.forename: Gemma L
authors.initials: GL
authors.lastname: Thomas
authors.forename: Yves S Y
authors.initials: YS
authors.lastname: Hsieh
authors.forename: Candy K Y
authors.initials: CK
authors.lastname: Chun
authors.forename: Zheng-Li
authors.initials: ZL
authors.lastname: Cai
authors.forename: Jeffrey R
authors.initials: JR
authors.lastname: Reimers
authors.forename: Richard J
authors.initials: RJ
authors.lastname: Payne
mesh_terms: D001224:Aspartic Acid / Q000737:chemistry*; D002384:Catalysis; D004952:Esters / Q000737:chemistry; D000077270:Exenatide; D018698:Glutamic Acid / Q000737:chemistry*; D007004:Hypoglycemic Agents / Q000138:chemical synthesis* / Q000737:chemistry; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D013237:Stereoisomerism; D013438:Sulfhydryl Compounds / Q000737:chemistry; D014688:Venoms / Q000138:chemical synthesis* / Q000737:chemistry
chemical_list: D004952:Esters; D007004:Hypoglycemic Agents; D010455:Peptides; D013438:Sulfhydryl Compounds; D014688:Venoms; D001224:Aspartic Acid; D018698:Glutamic Acid; D000077270:Exenatide