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Boehringer Ingelheim Foundation is funding research on “Structural basis of conformational misfolding of cystic fibrosis mutations in CFTR"

The group of Michael Schlierf is supported by an Exploration Grant of the Boehringer Ingelheim Foundation (BIS) to study the structural consequences of cystic fibrosis mutations in CFTR. Mutations in the amino acid sequence lead to cystic fibrosis (CF), the most common lethal genetic disease in Western populations. The large number of known loss of function mutations in CFTR causing the disease is not paralleled by our molecular understanding of the structure and folding of CFTR as well as how pathogenic mutations impair functioning of CFTR. In this project, structural studies on transmembrane hairpins reconstituted in liposomes will allow to capture heterogeneous structural ensembles. “We aim to develop a method based on FRET to capture structural changes induced by pathogenic mutations” , says Michael Schlierf. “Furthermore effects of pharmacochaperones on misfolded proteins will be explored to gain a fundamental understanding of their molecular mechanisms”. The project is funded for 18 months with a total budget of 80.000 EUR.

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