Published: 19-01-2018 09:28 | Updated: 30-03-2022 11:18

Michael Landreh, David Lane, Sonia Lain, Marcus Ladds et al publish in Cell Chemical Biology

In a study published in Cell Chemical Biology this week, researchers from MTC (Michael Landreh, David Lane, Sonia Lain, Marcus Ladds et al), KTH, Uppsala University, and the University of Oxford, used a new strategy to find out how anticancer drugs bind to the membrane protein dehydroorotate dehydrogenase (DHODH), a new cancer target.

The groups of Sir David Lane and Sonia Lain at the Department of Microbiology, Tumor and Cell Biology at Karolinska Institutet used native mass spectometry, a technique where a protein is gently removed from its normal environment and accelerated into a vacuum chamber. By measuring the time it takes for the protein to fly through the chamber, it is possible to determine its exact weight, which can, in turn, indicate whether the protein has bonded to another molecule and if so, what kind. The researchers used this highly accurate ”molecule scale” to see how drugs and lipids, the building blocks of the cell membrane, bind to DHODH.

Read the full news story here: Flying membrane protein aids cancer drug design