Chemical methods for N- and O-sulfation of small molecules, amino acids and peptides

Anna Mary Benedetti, Daniel Gill, Chi Tsang, Alan M Jones

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)
241 Downloads (Pure)


Sulfation of the amino acid residues of proteins is a significant post-translational modification, the functions of which are yet to be fully understood. Current sulfation methods are limited mainly to O-tyrosine (sY), which requires negatively charged species around the desired amino acid residue and a specific sulfotransferase enzyme. Alternatively, for solid-phase peptide synthesis, a de novo protected sY is required. Therefore, synthetic routes that go beyond O-sulfation are required. We have developed a novel route to N-sulfamation and can dial-in/out O-sulfation (without S-sulfurothiolation), mimicking the initiation step of the ping-pong sulfation mechanism identified in structural biology. This rapid, low-temperature and non-racemising method is applicable to a range of amines, amides, amino acids, and peptide sequences.

Original languageEnglish
Pages (from-to)938-942
Number of pages5
Issue number7
Early online date6 Nov 2019
Publication statusPublished - 1 Apr 2020

Bibliographical note

© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.


  • amino acids
  • sulfamation
  • sulfation
  • sulfopeptides
  • sulfurothiolation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry


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