Medizinische Universität Wien
A multitude of human diseases (e.g. cystic fibrosis) are due to mutations that lead to retention of the affected proteins in the endoplasmic reticulum, where they are recognized as misfolded by the quality control system. Facilitating the escape of the mutant proteins from the quality control system by the addition of chemicals that assist folding (chemical chaperones) can result in proteins that are fully functional despite their mutation.
Research in our group currently focuses on the identification and characterization of low molecular weight compounds that promote folding and transport of multispecific transmembrane transporters (e.g. P-glycoprotein).
The research project is embedded in a multidisciplinary environment (SFB35, www.sfb35.at) combining expertise in cellular, molecular, computational and chemical biology.
Institut für medizinische Chemie
Forschung & Lehre