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Application of gel‐phase 19 F NMR spectroscopy for optimization of solid‐phase synthesis of a hydrophobic peptide from the signal sequence of the mucin MUC1
Author(s) -
Pudelko Maciej,
Kihlberg Jan,
Elofsson Mikael
Publication year - 2007
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.850
Subject(s) - solid phase synthesis , peptide , chemistry , dipeptide , peptide synthesis , nuclear magnetic resonance spectroscopy , combinatorial chemistry , residue (chemistry) , phase (matter) , mucin , spectroscopy , stereochemistry , organic chemistry , biochemistry , physics , quantum mechanics
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.