1099-1387/asset/PSC_left.gif?v=1&s=8a12eca29ad625411fd707f9f6fdb57a8350cf0c)
1099-1387/asset/PSC_right.gif?v=1&s=181d84d31366428b2bf1cdbbd84306433ea461b3)
Research Article
Improved Fmoc-based solid-phase synthesis of homologous peptide fragments of human and mouse prion proteins
Article first published online: 16 SEP 2010
DOI: 10.1002/psc.1293
Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.
Additional Information
How to Cite
Grillo-Bosch, D., Rabanal, F. and Giralt, E. (2011), Improved Fmoc-based solid-phase synthesis of homologous peptide fragments of human and mouse prion proteins. J. Peptide Sci., 17: 32–38. doi: 10.1002/psc.1293
Publication History
- Issue published online: 19 DEC 2010
- Article first published online: 16 SEP 2010
- Manuscript Accepted: 29 JUL 2010
- Manuscript Revised: 23 JUL 2010
- Manuscript Received: 14 MAY 2010
Funded by
- MEC-FEDER. Grant Numbers: BIO2008-00799, CTQ2008-06200
- Generalitat de Catalunya
- Abstract
- Article
- References
- Cited By
Keywords:
- difficult sequence;
- prion protein;
- aggregation;
- PEGA resin
Abstract
The synthesis of difficult peptide sequences has been a challenge since the very beginning of SPPS. The self-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 (106–126) and MoPrP105–125 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 PEG-based resins as an efficient synthetic tool to prepare peptide sequences prone to aggregate on-resin. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.