Inimex Pharmaceuticals and SARomics Biostructures announce that they have achieved a scientific milestone in their collaboration to solve the structure of Inimex’s Innate Defense Regulator (IDR) IMX942 in complex with its target, the ZZ domain of human p62 (sequestosome-1).
No structures were previously available for this challenging protein domain. The crystal structure determined by SARomics Biostructures provides invaluable information that will assist the functional understanding of IMX942 and the development of the new generation of IDRs.
The p62 ZZ domain was cloned, expressed, purified and crystallized by SARomics Biostructures in collaboration with their molecular biology partner Vectron Biosolutions in Trondheim, Norway. Excellent crystallographic data were obtained at the MAX-lab synchrotron in Lund, Sweden.
“We are very excited to be able to help Inimex Pharmaceuticals fully leverage the potential of IMX942 by revealing the molecular details of its interactions with its target protein”, says Dr. Derek Logan, Chief Scientific Officer of SARomics Biostructures AB.
IMX942 is the first of a new class of drugs known as Innate Defense Regulators (IDRs), which improve survival, ameliorate tissue damage and reduce bacterial infections through modulation of innate defenses. IMX942 is a small, proprietary, fully synthetic peptide that binds to the intracellular adaptor protein p62 and modifies the signaling network downstream of TLR, TNF, and IL-1 receptors. IMX942 acts on the final common pathways of pathogenesis, being effective against antibiotic resistant infections and controlling the outcome of disease caused by a broad spectrum of pathogens, by chemotherapy and by localized radiation.
Inimex Pharmaceuticals
