Fmoc solid-phase synthesis of peptide thioesters using an intramolecularn,S-acyl shift.
[reaction: see text] We describe the Fmoc solid-phase synthesis of peptide thioesters based on the alkylation of the safety-catch sulfonamide linker with a protected 2-mercaptoethanol derivative. The thioester is generated on the solid phase after the peptide chain assembly as a consequence of an intramolecular N,S-acyl shift. Depending on the stability of the spacer separating the sulfonamide linker from the resin toward TFA, treatment of the peptidyl resin with TFA led to a soluble or supported deprotected thioester.
Ollivier
Nathalie
N
Institut Pasteur de Lille, Université de Lille 2, UMR 8525 CNRS, 1 rue du Professeur Calmette, 59021 Lille Cedex, France.
Behr
Jean-Bernard
JB
El-Mahdi
Ouafâa
O
Blanpain
Annick
A
Melnyk
Oleg
O
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D020650:Combinatorial Chemistry Techniques; D004952:Esters; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D000596:Amino Acids; D004952:Esters; D010455:Peptides