This year, an estimated 8,880 Utah residents will be diagnosed with cancer, according to the Huntsman Cancer Foundation. When you include friends and loved ones of patients, the number of individuals affected by cancer is much larger. The research of Professor Josh Price, of the Department of Chemistry and Biochemistry, is aimed at reducing that impact by enhancing the effectiveness of pharmaceutical drugs like those used to treat breast cancer and glaucoma.
Price, whose work at BYU focuses on protein structure and folding, began this line of research during his postdoctoral fellowship at The Scripps Research Institute. He recently published two articles on protein folding guidelines that could further stabilize and increase effectiveness of certain pharmaceutical drugs.
The first article appeared in the Proceedings of the National Academy of Sciences and proposed guidelines for linking a sugar to the protein chain in a way that makes the protein more stable.
Because the stomach easily digests protein, protein-based medications are administered via injection. Adding sugars to the protein chains could strengthen these medications, helping them to resist breakdown and to last longer in the bloodstream.
“Even once the medications are injected, your immune system can sometimes recognize the proteins as foreign, giving you an undesired immune response,” Price said. “Research has found that adding a sugar to a protein can help avoid all of those problems.”
Price’s second article, published in the journal ACS Chemical Biology, demonstrates that linking a polyethylene glycol (PEG) polymer to a protein can also increase protein stability.
“So what we’re doing now in my lab at BYU is following up on this observation to try to understand why PEG stabilizes the protein, what the rules are and if we can use them to our advantage,” he said.
These advances in protein research may someday be useful to the pharmaceutical industry. In 2010, six of the twenty top-selling drugs were protein based.
“Five of those [protein-based drugs] were antibodies, two were directed at autoimmune disease, and three directed at cancer,” Price said. “We believe that general strategies for enhancing protein stability could make these drugs even more effective.”