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Improved Fmoc-based solid-phase synthesis of homologous peptide fragments of human and mouse prion proteins

โœ Scribed by Dolors Grillo-Bosch; Francesc Rabanal; Ernest Giralt

Book ID
105359922
Publisher
John Wiley and Sons
Year
2010
Tongue
English
Weight
283 KB
Volume
17
Category
Article
ISSN
1075-2617

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โœฆ Synopsis

Abstract

The synthesis of difficult peptide sequences has been a challenge since the very beginning of SPPS. The selfโ€assembly of the growing peptide chains has been proposed as one of the causes of this synthetic problem. However, there is an increasing need to obtain peptides and proteins that are prone to aggregate. These peptides and proteins are generally associated with diseases known as amyloidoses. We present an efficient SPPS of two homologous peptide fragments of HuPrP (106โ€“126) and MoPrP105โ€“125 based on the use of the PEGA resin combined with proper coupling approaches. These peptide fragments were also studied by CD and TEM to determine their ability to aggregate. On the basis of these results, we support PEGโ€based resins as an efficient synthetic tool to prepare peptide sequences prone to aggregate onโ€resin. Copyright ยฉ 2010 European Peptide Society and John Wiley & Sons, Ltd.

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