In this new series, we wanted to provide a spotlight on some of our employees! Culture is an important part of OMass, so we want to show what it’s like to work here and what motivates OMassians to come to work every day.
Our second interviewee is Charlie Lay, who joined our pharmacology team as a scientist II back in July of 2022. Charlie joined us from University of Nottingham, where he did his PhD on the molecular pharmacology of the Interleukin-23 receptor. We can confirm his pharmacology skills are better than his kayaking!
How long have you been at the company and what is your favourite part of working here?
I have been at OMass for almost a year an half now. My favourite thing about being a part of OMass is the opportunity to work closely with a team of highly skilled scientists who have deep expertise in techniques I haven’t yet worked with during my career. Whether that’s the cutting-edge mass spectrometry assays or structural biology – the wealth of experience in our tightknit team allows us to explore how our drug targets work and how best to modulate them.
It’s exciting for me to be able to apply my pharmacology skillset in this context to provide proof of target engagement or helping elucidate the mechanism of action of different compound series.
What’s one thing that surprised you about your current role?
The freedom to approach difficult problems in innovative ways and to explore novel aspects of our drug targets. At OMass we have selected difficult to drug targets and so the understanding of the basic biology here is key. We are often asking questions that have not yet been asked in the literature and so the research leads us in exciting directions.
Explain OMass in three words
Innovative, Supportive, Exciting
When not at work, where would we likely find you?
Jogging, cycling or kayaking along the River Thames or in the Thames after I have capsized the kayak…
What is a cool paper that you have read recently?
Custodio and colleagues recently published a paper on the ‘Molecular basis of TASL recruitment by the peptide/histidine transporter 1 PHT1’ in Nature communications. I enjoyed reading their work as it combined alphafold prediction with other techniques including; Cryo-EM, micro-scale thermophoresis, co-immunoprecipitation and thermostablisation to learn more about how this important adaptor protein functions. It is a particularly interesting as so few papers have yet been published on the structural basis of the TASL:PHT1 interaction.
November 20, 2023
September 29, 2023
April 24, 2023