Chemical methods for N- and O-sulfation of small molecules, amino acids and peptides
Research output: Contribution to journal › Article
Sulfation of the amino acid residues of proteins is an emerging 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 are required to go beyond O ‐sulfation. 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‐racemizing method is applicable to a range of amines, amides, amino acids, and peptide sequences.
|Early online date||6 Nov 2019|
|Publication status||Published - 3 Jan 2020|
- sulfation, sulfamation, sulfurothiolation, sulfopeptide, modification