ERROR 1
ERROR 1
ERROR 2
ERROR 2
ERROR 2
ERROR 2
ERROR 2
Password and Confirm password must match.
If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)
ERROR 2
ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.
A new technique for detecting citrulline groups, a type of posttranslational protein modification associated with a variety of human diseases, has speed and sensitivity advantages over previous techniques (J. Am. Chem. Soc., DOI: 10.1021/ja308871v). The method could lead to a deeper understanding of citrullination and aid drug development for associated illnesses. Citrullines are amino acids generated from arginine residues by protein arginine deiminases (PADs), which have abnormally high activity in rheumatoid arthritis, ulcerative colitis, Alzheimer’s disease, multiple sclerosis, cancer, and other conditions. The role of citrullination isn’t well understood, in part because colorimetric detection of citrulline has low sensitivity and antibody-based detection techniques are expensive and slow. Paul R. Thompson of Scripps Florida and coworkers devised a phenylglyoxal-based citrulline test with fluorescence detection. The method is fast and highly sensitive, and it can be used by most researchers because the reagents and instruments needed for detection are available in virtually all biochemically focused laboratories, the researchers note. They used the technology to identify disease biomarkers in mice with ulcerative colitis and believe it could aid the search for therapeutic PAD inhibitors.
Join the conversation
Contact the reporter
Submit a Letter to the Editor for publication
Engage with us on X