Profile

I’m a first year PhD student, who recently started her adventure with research. I’m originally from Poland, and I moved to Edinburgh for my undergraduate degree. I have enjoyed the lovely (although very windy) city, and decided to stay on for a PhD.

I was always involved with a local drama group throughout my education (university included), and am a big theatre lover. I couldn’t name a favourite play (there is just too many!), but I have been enjoying National Theatre Live performances from the comfort of my sofa in lockdown.

Alzheimer’s, Parkinson’s and dementia are all diseases in which proteins in the human brain start acting up. Instead of playing their normal role, they start to “clump” together. This “clumping” makes the protein not functional, but is also harmful for the brain cells. In the “sticky” state the protein can attach to other things, and disrupt the normal functioning of the cell.

My work is trying to help understand what these protein “clumps” look like, what their features are, and how they can be formed within human brain. This is necessary to effectively diagnose and treat conditions like Alzheimer’s & Parkinson’s.

So how can we look at protein in the brain?

I am working on developing molecular labels that would be able to bind to the mis-behaving protein and show us where it is. I need to make sure the labels only bind to the protein I am interested in (as you can imagine, there is plenty other protein in the brain) and are able to detect the protein even in small(ish) amounts. The labels are very colourful and are “activated” by lasers. If I shine some light on them, they will also shine (fluoresce) a different colour – telling me that I found something interesting!

I test these labels under a special microscope (that I have helped build – I’ve never imagined I’d be using a screwdriver and a wrench as chemist before!). The microscope can gather a lot of data – it can show me a close up of a brain, and how bright the labelled protein is. It also records any changes in the colour of the label upon binding to the protein, and how the label becomes dimmer and dimmer over time (the fancy name for this property is “fluorescence lifetime”). This in turn, can help me reason about the structure of the protein “clump” – is it dense? Is it the same throughout the clump, or are the edges/centre a bit different?

It’s a fun project that shows me a couple of different sides of chemistry and science, and means I get to meet and work with a lot of experts from different fields.

As a scientist working in research, the most typical thing about my day is that I run experiments and analyse the data… usually to then plan some more experiments. What the experiments actually look like is a different story. This will change depending on the stage of the project, the question you are trying to answer, recent findings, opportunities for collaborations, and things/instruments available.

I work on molecules and techniques that can help us observe protein mis-behaviour, and actually have a couple of different laboratories for the different experiments I run. I synthesise molecules in a chemistry lab, but if I am testing molecules, I will usually be either in the “wet lab” (where we prepare samples, make solutions, work with brain tissue etc), or the optics lab (which is home to a couple of different microscopes that can collect all sorts of data).

The instrument that I use, Freddie (technical name FLIM – Fluorescence Lifetime Imaging Microscope, but I think we can agree Freddie just sounds better), is quite new! In fact there is only one other microscope like this (also at our university). It’s special because it lets me collect more information than any other instrument. It can see how bright the molecular labels I make are, but also can detect if they change colour when they bind to the protein I want to label. The microscope is also able to record “fluorescence lifetime” (how long it takes for the bright label to become dimmer over time). The more information I can get the better, because it helps me piece together what could be going on.

Once I am done running experiments, I am bound to spend some time on my laptop for the last bit of the afternoon – it’s important to take time to look over your results, make some pretty graphs, make sure you made the correct compound. It also helps planning the work for the next day: figuring out what information you are missing, what you can improve on, and what are the logical next steps.