Recent research into possible protein cross-linking yielded “quite significant” results, according to Dr. Shelly Kumar, university professor of chemistry. Dr. Kumar presented a poster display on the research at the October regional meeting of the American Chemical Society in Puerto Rico. He said fellow scientists at the conference appreciated the research, which Dr. Kumar conducted in GSU’s chemistry laboratory with graduate student Dineshkumar Dobariya. Kumar plans to confirm his findings, write a research paper, and submit it for publication in a peer-reviewed journal. The research was significant because it showed that a derivative of the amino acid histidine, when photooxidized, combined itself to create a dimer, which is a chemical compound formed when two smaller identical or similar molecules are linked together. The photooxidation conditions used in this experiment mimic the conditions under which proteins crosslink to cause cataract formation in the eye lens. Dr. Kumar said the experiment marked the first time such a dimer has been formed from histidine. “My research involves light and oxygen, and I mainly work with biological problems,” Dr. Kumar said. As a professor of organic chemistry, he prefers working with “small molecules” rather than large protein molecules. This strategy allows him to accomplish research work that is less tedious and less complicated. In his present research, he synthesized a derivative of histidine and showed formation of a dimer from it, while other researchers working with large protein molecules have had difficulty finding a dimer. This project is likely to have implications for medical research, Dr. Kumar said. For now, though, he expects the research will first be peer-reviewed and will lead to further experimentation. Dr. Kumar said he has been researching how protein compounds are oxidized for 10 years and, start to finish, this latest project took about two years.
