Eamonn obtained his MSci in Chemistry from the University of Bristol, where he performed research with Dr Wuge Briscoe and Dr Gareth Owen. He then went on to obtain a DPhil at the University of Oxford within the laboratory of Professor Dame Carol Robinson in 2015.
Eamonn then moved to King's College London as a post-doctoral researcher within the laboratory of Professor Paula Booth before, in 2016, becoming a BBSRC Future Leader Fellow.
Since 2019, Eamonn became a Lecturer in Chemistry at King's College London and was recently awarded a UKRI Future Leaders Fellowship.
Developing structural mass spectrometry tools for the determination of native membrane protein structural biology information. Using these developments to decipher the mechanisms of drug efflux for multidrug efflux transporters, which play major roles in antibiotic resistance.
Membrane proteins are ubiquitous biological macromolecules which reside within dynamic and highly complex cellular lipid membranes. They carry out a multitude of essential, complex biological functions with exquisite specificity within their cell membrane environment and concurrently are key targets for more than half of modern drugs. This makes understanding their fundamental processes a vital task. Currently, most of our structural insights on membrane proteins are gained within purified membrane mimetic systems which lack the context of the native lipid environment. Being able to achieve structural insight into these fundamental biomolecules within more native environments, including in live cells, would be a huge step forward in understanding how they shape cellular function.
Here, we develop structural mass spectrometry approaches to decipher native membrane protein structural behaviour, function, and biosynthesis. Emphasis is placed on understanding the role of drugs and the lipids on membrane protein behaviour. Importantly, we perform molecular biology and biochemical characterization alongside technology development to fully understand membrane protein behaviour and function. This is critical because high quality, functional biological samples are needed to be tailored to the mass spectrometry technology, and vice versa.
One area in which membrane proteins are important for health is in the development of antibiotic resistance, which has been linked to the function of multidrug efflux transporters. Our research currently focuses on multidrug efflux systems which play a major role in bacterial antibiotic resistance.
Please see the Reading Lab webpage for more information.
Publications could not be loaded at this time. Please try again later.