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Fmoc solid-phase synthesis of peptide thioesters using an intramolecularn,S-acyl shift
Nathalie Ollivier1, Jean-Bernard Behr, Ouafâa El-Mahdi
1Institut Pasteur de Lille, Université de Lille 2, UMR 8525 CNRS, 1 rue du Professeur Calmette, 59021 Lille Cedex, France.
Organic Letters
|June 17, 2005
Summary
We developed a new Fmoc solid-phase synthesis for peptide thioesters using a safety-catch sulfonamide linker. This method allows for the generation of soluble or resin-bound thioesters after peptide assembly.
Area of Science:
- Organic Chemistry
- Biochemistry
- Synthetic Chemistry
Background:
- Peptide thioesters are valuable intermediates in chemical biology and peptide synthesis.
- Current methods for solid-phase synthesis of peptide thioesters have limitations.
Purpose of the Study:
- To develop a novel and efficient method for the solid-phase synthesis of peptide thioesters.
- To utilize a safety-catch sulfonamide linker for thioester generation.
Main Methods:
- Fmoc (9-fluorenylmethoxycarbonyl) solid-phase synthesis was employed.
- Alkylation of a safety-catch sulfonamide linker with a protected 2-mercaptoethanol derivative was performed.
- Intramolecular N,S-acyl shift was utilized for thioester formation on the solid phase.
Main Results:
- Peptide thioesters were successfully synthesized on solid support.
- The method allows for the generation of either soluble or resin-bound deprotected thioesters.
- Cleavage conditions (TFA stability of the spacer) dictate the solubility of the final product.
Conclusions:
- This novel Fmoc solid-phase synthesis approach provides a versatile route to peptide thioesters.
- The method offers control over the final product's physical state (soluble or resin-bound).
- This strategy is valuable for various applications in peptide chemistry and bioconjugation.