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Functional Modification of Thioether Groups in Peptides, Polypeptides, and Proteins.

Timothy J Deming
Published in: Bioconjugate chemistry (2017)
Recent developments in the modification of methionine and other thioether-containing residues in peptides, polypeptides, and proteins are reviewed. Properties and potential applications of the resulting functionalized products are also discussed. While much of this work is focused on natural Met residues, modifications at other side-chain residues have also emerged as new thioether-containing amino acids have been incorporated into peptidic materials. Functional modification of thioether-containing amino acids has many advantages and is a complementary methodology to the widely utilized methods for modification at cysteine residues.
Keyphrases
  • amino acid
  • risk assessment
  • tyrosine kinase
  • high resolution
  • fluorescent probe
  • living cells
  • molecularly imprinted
  • liquid chromatography