Highly efficient solid phase synthesis of large polypeptides by iterative ligations of bis(2-sulfanylethyl)amido (SEA) peptide segments

Abstract : 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 (N3-Esoc linker) with the blocked thioester properties of SEAoff 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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Submitted on : Thursday, July 10, 2014 - 10:26:55 AM
Last modification on : Tuesday, June 4, 2019 - 4:30:10 PM

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Laurent Raibaut, Hélène Adihou, Rémi Desmet, Agnès F. Delmas, Vincent Aucagne, et al.. Highly efficient solid phase synthesis of large polypeptides by iterative ligations of bis(2-sulfanylethyl)amido (SEA) peptide segments. Chemical Science , The Royal Society of Chemistry, 2013, 4, pp.4061-4066. ⟨10.1039/c3sc51824h⟩. ⟨hal-00944814v2⟩

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