Going Round in Circles with N→S Acyl Transfer
| Autor: | Derek Macmillan |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
chemistry.chemical_classification
010405 organic chemistry Organic Chemistry Peptide 010402 general chemistry Hydrazide Thioester Native chemical ligation 01 natural sciences Combinatorial chemistry Cyclic peptide 0104 chemical sciences Amino acid chemistry.chemical_compound chemistry lipids (amino acids peptides and proteins) Peptide sequence Cysteine |
| Zdroj: | Synlett. 28:1517-1529 |
| ISSN: | 1437-2096 0936-5214 |
| DOI: | 10.1055/s-0036-1588789 |
| Popis: | It is not highly sophisticated, yet the N→S acyl transfer reaction of a native peptide sequence potentially fills an important technology gap. While several routes to synthetic peptide thioesters exist, only one is routinely applicable for biologically derived samples. Using the naturally occurring amino acid cysteine as the sole activator for N→S acyl transfer we have demonstrated transformation of synthetic and biologically derived precursors into thioesters for use in Native Chemical Ligation, providing a viable alternative for biological samples. Further refinement will be key to realising the full potential of this intriguing process, and increase the number of applications in peptide engineering and therapeutics.1 Introduction2 N→S acyl transfer in ‘normal’ peptide sequences3 Reduced reactivity of internal Xaa-Cys motifs as an advantage in head-to-tail peptide cyclisation4 Reduced reactivity of internal Xaa-Cys motifs as an advantage in modification and cyclisation of biologically produced precursors5 Hydrazinolysis of Xaa-Cys motifs and the acyl hydrazide as a stable thioester equivalent6 Rapid thioester formation via an N→Se acyl shift7 Outlook and conclusions |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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