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Application of gel-phase 19F NMR spectroscopy for optimization of solid-phase synthesis of a hydrophobic peptide from the signal sequence of the mucin MUC1

✍ Scribed by Maciej Pudelko; Jan Kihlberg; Mikael Elofsson

Book ID
105360673
Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
292 KB
Volume
13
Category
Article
ISSN
1075-2617

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✦ Synopsis

Abstract

This paper describes the manual Fmoc/t‐Bu solid‐phase synthesis of a difficult nine‐residue hydrophobic peptide LLLLTVLTV from one of the signal sequences that flank the tandem repeat of the mucin MUC1. Gel‐phase ^19^F NMR spectroscopy was used as a straightforward method for optimization of the solid‐phase synthesis. Different approaches were applied for comparative studies. The strategy based on modified solid‐phase conditions using DIC/HOAt for coupling, DBU for Fmoc deprotection, and the incorporation of the pseudo proline dipeptide Fmoc‐Leu‐Thr(ψ^Me, Me^ pro)‐OH as a backbone‐protecting group was found to be superior according to gel‐phase ^19^F NMR spectroscopy. Implementation of the optimized Fmoc protocol enabled an effective synthesis of signal peptide LLLLTVLTV. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.

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