Journal
CHEMICAL RECORD
Volume 12, Issue 5, Pages 479-490Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/tcr.201200007
Keywords
native chemical ligation; peptides; protein chemistry; sequential ligation; thioesters
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Funding
- KAKENHI
- Takeda Science Foundation
- Yoshida Scholarship Foundation
- Grants-in-Aid for Scientific Research [24102521, 23659055, 23390026, 24590010, 24390026] Funding Source: KAKEN
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N-Sulfanylethylanilide (SEAlide) peptides were developed with the aim of achieving facile synthesis of peptide thioesters by 9-fluorenylmethyloxycarbonyl (Fmoc)-based solid-phase peptide synthesis (Fmoc SPPS). Initially, SEAlide peptides were found to be converted to the corresponding peptide thioesters under acidic conditions. However, the SEAlide moiety was proved to function as a thioester in the presence of phosphate salts and to participate in native chemical ligation (NCL) with N-terminal cysteinyl peptides, and this has served as a powerful protein synthesis methodology. The reactivity of a SEAlide peptide (anilide vs. thioester) can be easily tuned with or without the use of phosphate salts. This interesting property of SEAlide peptides allows sequential three-fragment or unprecedented four-fragment ligation for efficient one-pot peptide/protein synthesis. Furthermore, dual-kinetically controlled ligation, which enables three peptide fragments simultaneously present in the reaction to be ligated in the correct order, was first achieved using a SEAlide peptide. Beyond our initial expectations, SEAlide peptides have served in protein chemistry fields as very useful crypto-peptide thioesters. DOI 10.1002/tcr.201200007
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