Serious conditions, including sepsis, stem from inflammation in the body, and there is a lack of effective medication for sepsis. A chromosomal protein called high-mobility group box 1 (HMGB1), secreted by immune and dying cells, binds to a specific cellular receptor—receptor for advanced glycation end-products (RAGE)—and triggers the process of inflammation in the body. Through a computer software-based docking study with a structural similarity-based strategy, scientists from Japan, led by senior researcher Prof Sei-ichi Tanuma from Tokyo University of Science (TUS), discovered that the popular anticonvulsant drug papaverine blocks the binding of HMGB1 to this receptor. This kind of "drug repositioning" can be used to find other merits for existing drugs whose safety profiles are known. This novel approach used for the first time here is unique to TUS and is described in the paper published in Biochemical and Biophysical Research Communications. Prof Tanuma states, "Our research group has been trying to identify compounds, preferably based on existing drugs, that block the binding of irritants to cellular receptors. We want to find novel drugs to treat inflammation-based conditions."
* This article was originally published here
