| Autor: |
Michael Bienert, Calin Dan Sferdean, Irene Coin, Eberhard Krause, Michael Beyermann, Louis A. Carpino, Sandra Tremmel |
| Rok vydání: |
2006 |
| Předmět: |
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| Zdroj: |
Understanding Biology Using Peptides ISBN: 9780387265698 |
| DOI: |
10.1007/978-0-387-26575-9_68 |
| Popis: |
Introduction While inspecting the crude product from a “difficult” peptide synthesis, we observed a group of isomeric analogs that were subsequently identified as the corresponding N,O-shift isomers. Surprisingly, the extent of N→O shift depends on the peptide sequence and even TFA may give rise to large amounts of depsipeptide by-products [1]. Interestingly, the presence of the ester linkage helped dramatically to overcome synthesis problems as also reported by other groups [2-4]. We have now compared the novel approach with the well-known pseudo-proline method [5], applying both to the synthesis of FBP-28 WW domain peptides. FBP-28 WW domain is a 37 residue peptide that belongs to the family of WW domains showing triple stranded, anti-parallel β-sheet structure in aqueous solution. Standard Fmoc-SPPS of the FBP-28 WW domain failed, probably due to its tendency to associate during assembly as well as aspartimide formation. The N15D analog of the wild type is a good model of a “difficult” peptide GATAVSEWTEYKTANGKTYYYNNRTLESTWEKPQELK. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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