Fresh data on protein interactions in Alzheimer’s disease

Professor Sara Linse will highlight the Fluidity One-W as an influential technology for protein interaction analysis during plenary lecture at FEBS 2019.

Demonstrates the unique ability of diffusional sizing to assess protein binding in-solution and for difficult-to-study systems.

Fluidic Analytics will host an extended Q&A session with Professor Linse at their booth (number 7) at 3 pm following her plenary talk. Visitors to the Fluidic Analytics booth will also be able to have an early look at the Fluidity One-W before its official launch later this year. This instrument has the ability to assess on-target protein interactions in solution and in crude biological backgrounds – opening up the possibilities for detailed analysis of proteins in their near-native states and natural environments. The system is easy-to-use, and based on the well-understood relationship between size and diffusion rate, providing researchers with true confidence in the quality and accuracy of their data.

Professor Sara Linse, Department of Biochemistry and Structural Biology, Lund University commented: “During our research into protein amyloid formation, we have used many different techniques for assessing protein interactions – all with different limitations and advantages. With diffusional sizing, we were able to confidently generate accurate and complete in-solution data using amyloid proteins to connect stoichiometry and binding affinities with protein self-assembly. The data we will present at FEBS 2019 could provide key insights for novel therapeutic approaches in Alzheimer’s disease. The Fluidity One-W has contributed significantly to this detailed understanding.”

With applications ranging from neurobiology and cell signalling to drug discovery, the potential impact of diffusional sizing in fundamental scientific research is vast and spans many research areas. Dr Sean Devenish, Head of R&D at Fluidic Analytics explained: “The unique capabilities of the Fluidity One-W position it as the only viable option for analysing difficult-to-study proteins, like amyloid fibrils, in solution. Researchers gain the best insight into what their protein of interest is interacting with, and how, even in complex backgrounds such as crude lysates. The technology is opening up many new avenues of research into protein interactions and expanding the systems that can be studied, and Professor Linse’s recent work is a great example of what’s possible with this new approach to protein analysis.”