Native N-glycopeptide thioester synthesis through N→S acyl transfer
2011

Synthesis of N-glycopeptide thioesters

publication Evidence: moderate

Author Information

Author(s): Premdjee Bhavesh Adams, Anna L. Macmillan, Derek Macmillan

Primary Institution: University College London

Hypothesis

Can N-glycopeptide thioesters be effectively synthesized through N→S acyl transfer?

Conclusion

Thioester formation via N→S acyl transfer is compatible with native N-glycopeptides and can be used for glycoprotein assembly.

Supporting Evidence

  • Peptide thioesters are important for protein synthesis.
  • The study demonstrated the compatibility of thioester formation with native N-glycopeptides.
  • Lowering the reaction pH inhibited NCL, which is beneficial for thioester production.

Takeaway

The study shows a way to make special building blocks for proteins using a new method that helps keep the sugar parts safe.

Methodology

The study involved preparing model N-glycopeptides and testing thioester formation under various conditions.

Limitations

The isolated yield of thioester formation was low (20-40%), and the reaction conditions may not be optimal for all scenarios.

Digital Object Identifier (DOI)

10.1016/j.bmcl.2011.05.059

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