Journal
CHEMICAL SCIENCE
Volume 4, Issue 10, Pages 4061-4066Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3sc51824h
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Funding
- ANR [12-EMMA-0006-01, JCJC08-0138]
- Region Nord Pas-de-Calais council
- Region Centre council
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Up to now, the advantages of solid phase protein synthesis have been largely under-utilized due to the difficulty of designing a simple and efficient elongation cycle enabling the concatenation of unprotected peptide segments. The combination of selective N-terminal anchoring (N-3-Esoc linker) with the blocked thioester properties of the SEA(off) group enabled the solid phase concatenation of unprotected peptide segments by N-to-C sequential formation of native peptide bonds. The strategy was applied to the synthesis of a 60 amino acid-long latent peptide thioester or to the assembly of five peptide segments to give a 15 kDa polypeptide.
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