Meet Margeoux

Here we introduce, Margeoux Dela Rosa the latest member of our membrane protein team and we start with Margeoux giving us a brief overview of her scientific journey.

"It was the final year of my integrated Masters at the University of Southampton where I realised: I loved being in the lab and doing scientific research. Shortly after my degree, I landed an internship at CRUK TDL where I gained invaluable experience in cell culture and immunobiology – a subject I find truly fascinating. Immediately after my internship, I started my PhD at UEA where I had the opportunity to supplement my basic biochemistry and membrane biology skills obtained from my Masters. Upon starting my PhD, I soon realised that the protein that I would be working on was closely linked to the subject of my internship project at CRUK. I wanted to marry the biochemistry of this protein to the proposed cellular functions (which remains widely disputed). However, a worldwide pandemic ensued for most of my PhD, so trying to tackle a challenging research question on a predominantly shift-work basis with minimal assistance was a bit difficult.

As I said before, I love being in the lab and doing scientific research and fortunately a PhD during a pandemic did not completely break that spirit. I applied for several lab-based research roles, all academic, until I decided to widen the net and apply to Sygnature. It was the first industry role that I applied for post-PhD, and I was a bit apprehensive because the nature of research in industry was unknown to me. But having a colleague who works in the company helped put my anxious thoughts at ease. Now that I'm here, I realised working at Sygnature is like a happy hybrid between academia and industry – which I'm pleased about because I get the best of both worlds".

1. What did you do before joining the Protein Sciences team at Sygnature?

Before joining the Protein Sciences team at Sygnature, I completed my PhD at UEA where my project focused on investigating the role of the mitochondrial carrier protein, UCP2, which has been implicated in various metabolic disorders. This protein was observed to have 59% similarity with another protein, UCP1, which is well-characterised. Whilst there has been a lot of research into these proteins, the sea of literature is quite "muddy" as there is a lot of conflicting data and the debate on what UCP2 does. My PhD aimed to clarify this through biochemical investigations.

Having done a Masters project in bacterial membrane protein characterisation, I understood the general pipeline required for protein expression and purification: design a tagged-protein construct, transform them into cells, express and purify protein to do the fun biochemical experiments. One major challenge that I faced during my PhD project, was the belief that these proteins poorly tolerated the addition of purification tags, so I had to try and purify this protein without resorting to conventional affinity chromatography. To this end, I adapted a method (several times) that had been developed which could purify untagged versions of the closely related UCP1 protein, to try and purify UCP2. Whilst there was UCP2 protein in my final purified samples, the sample wasn't pure enough for conventional biochemical characterisation.

But I was determined to an inkling of new information about this protein before the end of my PhD. So, I set out to investigate UCP2's ligand binding properties, as it was believed to bind the same effectors as UCP1, due to its high protein sequence similarity. During my PhD, the main method used to probe into ligand binding is thermostability assay – with a maleimide-based fluorescent dye being the main method utilised for membrane proteins. Using the similar principles as well-established assays, I developed a thermostability assay that was capable of probing ligand-binding properties of proteins in unpurified systems through Western blotting. Through this new method, it was found that UCP2 did not bind the same ligands as UCP1, despite countless papers stating that it does! It was a clutch at the end, but I found this very "out-the-box" thinking very rewarding as it has a wide variety of applications, making it a potentially versatile technique.

2. What are you looking forward to about transitioning into your new role?

I know this sounds odd, but I'm excited to be one of the least experienced people in the company. Whilst it might be daunting for some, for me it means that I get to level up my experience – from purifying a variety of different proteins to working in a bigger company that deals with clients. I'm eager to work collaboratively in a super supportive environment, where I get the opportunity to soak in all the expertise from everyone around me. Essentially, I'm looking forward to growing both personally and professionally.

3. What do you find exciting about scientific research?

What I find exciting about scientific research is that it pushes the boundaries of what we know. In that respect, I love how science isn't really set in stone as we're always learning about new things which challenges the status quo and I'm all for questioning that.

4. What do you do in your spare time?

I'm a big foodie so I love to cook! (Not sure if this is because I find cooking analogous to being in the lab). When I'm not too busy trying to catch up with old friends, I'm trying to make the most of my move up to Macclesfield by taking hikes in and around the Peak District.