CHICAGO, March 14 (UPI) -- University of Illinois chemists have found a new way to bind compounds called ligation reactions that are useful in biological and medical research.
The researchers -- lead author Professor David Crich, graduate student Venkataramanan Krishnamurthy and post-doctoral researcher Thomas Hutton -- modified a common reaction called a disulfide ligation, used to bridge the amino acid cysteine with a related sulfur-containing compound called a thiol.
"It's done in water and at room temperature and is widely applied by biochemists to conjugate all kinds of molecules onto proteins to make haptens for antibody generation," said Crich. "It has many applications."
But the disulfide ligation is not permanent, said Crich, which limits its usefulness in developing new medicines. Crich's goal is to devise a room-temperature, water-based method to do protein glycosylation -- basically the process of hanging carbohydrate groups onto proteins.
The scientists report their findings in the March 1 issue of the Journal of the American Chemical Society.
