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Journal of Peptide Science

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Volume 13, Issue 12 , Pages 833 - 838

Published Online: 29 Aug 2007

Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.

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European Peptide Symposium
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 Research Article
Fast Fmoc synthesis of hAmylin1-37 with pseudoproline assisted on-resin disulfide formation
Karen Page, Christina A. Hood, Hirendra Patel, German Fuentes, Mahendra Menakuru, Jae H. Park *
Department of Chemistry, Protein Technologies Inc., Tucson, Arizona, 4675 South Coach Drive, Tucson, Arizona, 85714, USA
email: Jae H. Park (info@peptideinstruments.com)

*Correspondence to Jae H. Park, Department of Chemistry, Protein Technologies Inc., Tucson, Arizona, 4675 South Coach Drive, Tucson, Arizona, 85714, USA

Keywords
fast Fmoc SPPS • human amylin1-37 • pseudoproline dipeptide • disulfide bridge

Abstract
Human amylin (1-37) and the (1-13) fragment were synthesized with and without pseudoproline dipeptides. Thallium (III) trifluoroacetate, a mild oxidant, was used to cyclize the peptides by forming a disulfide bridge from C2 to C7. On the basis of our model studies, incorporation of a pseudoproline dipeptide decreases the amount of time necessary for the crude linear amylin (1-13) to cyclize on the resin. Without pseudoproline dipeptides, the 1-37 crude linear amylin was not pure enough to undergo the cyclization reaction. Following the cyclization studies, the synthesis time of the linear human amylin (1-37) was systematically reduced from 58 h to 8.5 h by shortening the reaction times. Cyclization and cleavage times were also reduced to 1.5 h. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.

Received: 8 May 2007; Revised: 15 June 2007; Accepted: 24 June 2007

Digital Object Identifier (DOI)

10.1002/psc.909  About DOI

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