Cysteine-Derived <i>S</i>-Protected Oxazolidinones:  Potential Chemical Devices for the Preparation of Peptide Thioesters

Ohta, Yusuke; Itoh, S; Shigenaga, Akira; Shintaku, Saori; Fujii, Nobutaka; Otaka, Akira

doi:10.1021/ol052755m

Cited by 99 publications

(45 citation statements)

References 31 publications

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“…Thus, methylation of the thiol group prior to TFA treatment was required for its complete removal. As N-S acyl shift from the secondary amino group under acidic condition is known (36)(37)(38)(39), care has to be taken for the final deprotection, when these auxiliary groups are used.…”

Section: Solution To the Restriction Of Ligation Site In Ncl Methodsmentioning

confidence: 99%

“…Recently, several groups including us have developed post SPPS thioesterification methods via N-to S-acyl shift reaction (36)(37)(38)(39). As the peptide chain is stably immobilized by the amide bond to the resin during SPPS and no activation such as alkylation is required for thioesteri-fication, these methods realize simple and high yield synthesis of peptide thioester.…”

Section: Scheme 3 Schemementioning

confidence: 99%

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Progress in the Ligation Chemistry for Glycoprotein Synthesis

Hojo

Katayama

Nakahara

2010

TIGG

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Section: Solution To the Restriction Of Ligation Site In Ncl Methodsmentioning

confidence: 99%

Section: Scheme 3 Schemementioning

confidence: 99%

Progress in the Ligation Chemistry for Glycoprotein Synthesis

Hojo

Katayama

Nakahara

2010

TIGG

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“…This post-SPPS thioesterification reaction was successfully applied to the synthesis of a glycopeptide thioester. N-alkyl cysteine derivatives were also used for the preparation of peptide thioesters [69,70]. Tsuda reported N ?…”

Section: Nclmentioning

confidence: 99%

Progress in Chemical Synthesis of Peptides and Proteins

Hou

Zhang

Liu

2017

Trans. Tianjin Univ.

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For the proteins that cannot be expressed exactly by cell expression technology (e.g., proteins with multiple posttranslational modifications or toxic proteins), chemical synthesis is an important substitute. Given the limited peptide length offered by solid-phase peptide synthesis invented by Professor Merrifield, peptide ligation plays a key role in long peptide or protein synthesis by ligating two small peptides to a long one. Moreover, high-molecularweight proteins must be synthesized using two or more peptide ligation steps, and sequential peptide ligation is such an efficient way. In this paper, we reviewed the development of chemical protein synthesis, including solid-phase peptide synthesis, chemical ligation, and sequential chemical ligation.

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“…To avoid these problems, several groups have explored indirect methods of peptide thioester synthesis, in which a thioester bond is formed after the peptide chain is assembled21–39. Safety catch strategy is now widely used in Fmoc‐based peptide thioester synthesis, but some problems have been reported, including methionine ε‐cyanilation (approx.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of peptide thioesters via an N–S acyl shift reaction under mild acidic conditions on an N‐4,5‐dimethoxy‐2‐mercaptobenzyl auxiliary group

Ken'ichiroh

Kanao

Uesugi

et al. 2009

Journal of Peptide Science

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An efficient method of peptide thioester synthesis is described. The reaction is based on an N-4,5-dimethoxy-2-mercaptobenzyl (Dmmb) auxiliary-assisted N-S acyl shift reaction after assembling a peptide chain by Fmoc-solid phase peptide synthesis. The Dmmb-assisted N-S acyl shift reaction proceeded efficiently under mildly acidic conditions, and the peptide thioester was obtained by treating the resulting S-peptide with sodium 2-mercaptoethanesulfonate. No detectable epimerization of the amino acid residue adjacent to the thioester moiety in the case of Leu was found. The reactions were also amenable to the on-resin preparation of peptide thioesters. The utility was demonstrated by the synthesis of a 41-mer peptide thioester, a phosphorylated peptide thioester and a 33-mer peptide thioester containing a trimethylated lysine residue.

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Cysteine-Derived S-Protected Oxazolidinones: Potential Chemical Devices for the Preparation of Peptide Thioesters

Abstract: [reaction: see text]. An N-S acyl-transfer-mediated preparation of peptide thioesters using the S-protected oxazolidinone derived from cysteine has been developed and applied to the synthesis of a 32-mer biologically active peptide by native chemical ligation protocols.

Cited by 99 publications

References 31 publications

Progress in the Ligation Chemistry for Glycoprotein Synthesis

Progress in the Ligation Chemistry for Glycoprotein Synthesis

Progress in Chemical Synthesis of Peptides and Proteins

Synthesis of peptide thioesters via an N–S acyl shift reaction under mild acidic conditions on an N‐4,5‐dimethoxy‐2‐mercaptobenzyl auxiliary group

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