title: Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide.
abstract: The efficient Fmoc solid-phase peptide synthesis of the 37-residue human Amylin and its amyloidogenic 8-37 fragment was achieved using pseudoproline (oxazolidine) dipeptide derivatives. Syntheses of hAmylin(8-37) using Fmoc amino acids produced only traces of the desired peptide. Incorporation of pseudoproline dipeptides produced the desired product with high yield and allowed for the synthesis of the full length peptide. The crude material was pure enough to allow formation of the Cys-2 to Cys-7 disulfide by air oxidation. [Structure: see text]
authors.affiliation: Department of Chemistry, Graduate Program in Biochemistry and Structural Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-3400, USA.
authors.forename: Andisheh
authors.initials: A
authors.lastname: Abedini
authors.forename: Daniel P
authors.initials: DP
authors.lastname: Raleigh
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000138:chemical synthesis* / Q000737:chemistry; D004151:Dipeptides / Q000138:chemical synthesis; D006801:Humans; D058228:Islet Amyloid Polypeptide; D008969:Molecular Sequence Data; D010080:Oxazoles; D011392:Proline / Q000031:analogs & derivatives*; D013844:Thiazoles
chemical_list: D000682:Amyloid; D004151:Dipeptides; D058228:Islet Amyloid Polypeptide; D010080:Oxazoles; D013844:Thiazoles; C505976:pseudoproline; C064210:oxazolidine; D011392:Proline