Accessing protein methyltransferase and demethylase enzymology using microfluidic capillary electrophoresis.

ABSTRACT: The discovery of small molecules targeting the >80 enzymes that add (methyltransferases) or remove (demethylases) methyl marks from lysine and arginine residues, most notably present in histone tails, may yield unprecedented chemotherapeutic agents and facilitate regenerative medicine. To better enable chemical exploration of these proteins, we have developed a highly quantitative microfluidic capillary electrophoresis assay to enable full mechanistic studies of these enzymes and the kinetics of their inhibition. This technology separates small biomolecules, i.e., peptides, based on their charge-to-mass ratio. Methylation, however, does not alter the charge of peptide substrates. To overcome this limitation, we have employed a methylation-sensitive endoproteinase strategy to separate methy

SUBMITTER: Wigle TJ 

PROVIDER: S-EPMC2914686 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature