Publications by authors named "Arron Aatkar"
Sulfur(VI) fluorides (SFs) have emerged as valuable electrophiles for the design of "beyond-cysteine" covalent inhibitors and offer potential for expansion of the liganded proteome. Since SFs target a broad range of nucleophilic amino acids, they deliver an approach for the covalent modification of proteins without requirement for a proximal cysteine residue. Further to this, libraries of reactive fragments present an innovative approach for the discovery of ligands and tools for proteins of interest by leveraging a breadth of mass spectrometry analytical approaches.
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- This study explores sulfur(VI) fluorides (S-Fs) as reactive chemical groups that can modify important amino acids like lysine, tyrosine, histidine, and serine in proteins.
- Different types of S-Fs were tested for their stability and how effectively they react with specific amino acid sidechains.
- The research shows that S-Fs can be used in living cells to identify new protein targets, demonstrating their potential to enhance our understanding of the proteome.