ETH team decodes protein interactions

According to a press release, researchers led by Paola Picotti, Professor of Molecular Systems Biology at ETH Zurich, have succeeded in analyzing the various interactions of proteins in the cell fluid. To this end, they have further developed their Limited Proteolysis (LiP) mass spectrometry, which they developed several years ago. Altered interactions between proteins can lead to diseases such as Alzheimer's, Parkinson's or cancer.

"It is therefore important to know how protein-protein interactions differ between healthy and diseased states and what the binding sites between two proteins are like," explains PhD student Cathy Marulli. "If we know these down to the last detail, we can develop active substances that block unwanted interactions and restore the cell's balance."

To this end, the biochemists initially used yeast cells in their study to identify around 6000 interaction interfaces between proteins and other sites that change when proteins interact with each other. They then used these sites as markers to assess whether a protein changes its interaction with other proteins under a certain condition. In this way, they were able to study the interactions of around 1000 proteins simultaneously in a disordered cell matrix.

According to Marulli, any organism can be analyzed with a specific set of binding markers. "We therefore want to further develop our technology for diagnostic purposes and for researching disease mechanisms," says Picotti. Earlier approaches developed in her laboratory had already been transferred into practice by the ETH spin-off Biognosys, based in the Bio-Technopark Schlieren-Zurich. ce/mm