Carol Robinson Awarded 2024 Lifetime Achievement European Inventor Award

Carol Robinson, professor of Chemistry from the University of Oxford, has received the 2024 European Inventor Award for Lifetime Achievement from the European Patent Office. She is the first ever British recipient of the award.

Carol Robinson of the University of Oxford.

Robinson's work in mass spectrometry and structural biology has improved our understanding of protein interactions. Her early work challenged the prevailing belief that proteins could not maintain structure outside of water. However, Robinson's determination and innovative approach to analysis proved that protein interactions could indeed be preserved and studied in the gaseous state. Robinson’s native mass spectrometry technique preserves proteins in their natural state, allowing scientists to gain detailed insights into their functions and interactions without altering their structures. It enables precise measurements and analyses of protein complexes that play critical roles in various diseases. This breakthrough paved the way for the development of targeted medications that can address disease mechanisms more effectively than ever before.

“I've always been interested in drug discovery ever since I was a teenager working at Pfizer in the spectrometry section. So, in a way, I've been full circle, starting with very small molecules and now looking at the very big proteins with which they interact,” Robinson told LCGC International in an interview.

Robinson graduated from the Royal Society of Chemistry in 1979 and completed her PhD at the University of Cambridge. In 2001, she became the first woman professor of chemistry at the University of Cambridge (2001-2009). She has held the position of Dr. Lee’s Chair in Chemistry since 2009 and is Oxford University’s first woman professor of Chemistry. She is also the first director of the Kavli Institute for Nanoscience Discovery at Oxford.

“My first published work in my own laboratory was really published in the mid-1990s, and I was very excited to publish something where I first talked about protein complexes directly from living systems. I thought that was really very exciting. I don't think many people paid it much attention, but I I'm proud of it still,” Robinson says.

Robinson’s early work challenged the prevailing belief that proteins could not maintain structure outside of water, she said. Through her research, Robinson and her team were able to show that by using electron microscopy, the overall structure of these proteins can be maintained outside of water.

“The central tenet of our research is that native mass spectrometry (MS), a technique which enables interactions of proteins to be maintained in the gas phase, can provide unparalleled information on the structure, binding partners and dynamics of proteins, complementing other biophysical approaches yet a powerful tool in its own right,” Robinson said (1).

Robinson has also been recognized for establishing mass spectrometry as a viable technology to study the structure, function and interactions of proteins. Her collaborations span both academic and industrial laboratories and in 2016 she founded her company, OMass Technologies. Now trading as OMass Therapeutics, the company uses high-definition native mass spectrometry to develop drug therapies for use in immunologic and genetic disorders (1).

Published Research

Robinson’s research spans a variety of topics including recapitulating physiological environments using novel detergents and membrane mimetics, ejecting complexes directly from membranes, uncovering mechanisms of drug resistance, linking post-translational modifications to function of protein complexes, and Trapping metabolites in membrane proteins to link protein complexes to health disorders.

For an example of Robinson recently published a study “Phage defence system CBASS is regulated by a prokaryotic E2 enzyme that imitates the ubiquitin pathway” in Nature Microbiology This study uses biochemical, genetic, cryo-electron microscopy and mass spectrometry to investigate the E2 enzyme and how it regulates cyclicguanosine monophosphate–adenosine monophosphate(GMP-AMP) synthase (cGAS) in the immune system, specifically the cyclic-oligonucleotide-based anti-phage signaling system (CBASS).

Another study published in the Journal of the American Chemical Society centers around lipopolysaccharide (LPS), which helps maintain the outer membrane barrier in Gram-negative bacteria (3). In this study, the scientists leveraged the control of the hydrophilic-lipophilic balance and packing parameter concepts to chemically tune detergents that can be used to qualitatively differentiate the degree to which proteins copurify with phospholipids (PLs) or LPS. They concluded that LPS can also affected the activity of membrane proteins currently unassigned to be involved in outer membrane biogenesis.

Moving forward, Robinson and her team are continuing to research the intricacies of mental health. There is much to learn about this and mass spectrometry research, and Robinson said that she looks forward to seeing what growth can be made in this area.

“We're still working on trying to understand this connection between different neurosecretory cells in the brain and depression. So, this is very exciting for me,” she said.

References

(1) Professor Dame Carol Robinson DBE FRS FMedSci FRSC. University of Oxford 2024. https://www.chem.ox.ac.uk/people/dame-carol-robinson#tab-2633146 (accessed 2024-7-24)

(2) Yan, Y.; Xiao, J.; Huang, F.; Xian, W.; et al. Phage Defence System CBASS is Regulated by a Prokaryotic E2 Enzyme That Imitates the Ubiquitin Pathway. Nat. Microbiol. 2024, 9, 1566–1578. DOI: 10.1038/s41564-024-01684-z

(3) Umer, L. H.; Fiorentino, F.; Shutin, D.; Sauer, J. B.; et al. Detergents with Scalable Properties Identify Noncanonical Lipopolysaccharide Binding to Bacterial Inner Membrane Proteins. J. Am. Chem. Soc. 2024, 146 (16), 11025–11030. DOI: 10.1021/jacs.3c14358