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Org Lett. 2005 Feb 17;7(4):693-6.

Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide.

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Department of Chemistry, Graduate Program in Biochemistry and Structural Biology, State University of New York at Stony Brook, Stony Brook, NY 11794-3400, USA.


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].

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