1034403-62-7Relevant academic research and scientific papers
Trifluoroethanethiol: An additive for efficient one-pot peptide ligation - Desulfurization chemistry
Thompson, Robert E.,Liu, Xuyu,Alonso-García, Noelia,Pereira, Pedro José Barbosa,Jolliffe, Katrina A.,Payne, Richard J.
supporting information, p. 8161 - 8164 (2014/06/24)
Native chemical ligation followed by desulfurization is a powerful strategy for the assembly of proteins. Here we describe the development of a high-yielding, one-pot ligation-desulfurization protocol that uses trifluoroethanethiol (TFET) as a novel thiol additive. The synthetic utility of this TFET-enabled methodology is demonstrated by the efficient multi-step one-pot syntheses of two tick-derived proteins, chimadanin and madanin-1, without the need for any intermediary purification.
Solid-phase synthesis of peptide and glycopeptide thioesters through side-chain-anchoring strategies
Ficht, Simon,Payne, Richard J.,Guy, Richard T.,Wong, Chi-Huey
experimental part, p. 3620 - 3629 (2009/05/27)
An efficient new strategy for the synthesis of peptide and glycopeptide thioesters is described. The method relies on the side-chain immobilization of a variety of Fmoc-amino acids, protected at their C-termini, on solid supports. Once anchored, peptides were constructed using solid-phase peptide synthesis according to the Fmoc protocol. After unmasking the C-terminal carboxylate, either thiols or amino acid thioesters were coupled to afford, after cleavage, peptide and glycopeptide thioesters in high yields. Using this method a significant proportion of the proteinogenic amino acids could be incorporated as C-terminal amino acid residues, therefore providing access to a large number of potential targets that can serve as acyl donors in subsequent ligation reactions. The utility of this methodology was exemplified in the synthesis of a 28 amino acid glycopeptide thioester, which was further elaborated to an N-terminal fragment of the glycoprotein erythropoietin (EPO) by native chemical ligation.
