Dr Mathew H Horrocks
The use and development of single-molecule and super-resolution microscopy to answer biological questions, with a focus on neuroscience and neurodegeneration.
- Takeshi Kaizuka (PDRA)
- Ji-Eun Lee (PDRA)
- Rebecca Saleeb (Motor Neurone Disease Association Research Fellow)
- Craig Leighton (PDRA)
- Dylan George (PDRA)
- Judi O'Shaughnessy (Histology Technician)
- Candace Adams (PhD Student)
- Haresh Bhaksar (PhD Student)
- Noelia Pelegrina-Hidalgo (PhD Student)
- Zuzanna Konieczna (PhD Student)
- Katie Morris (PhD Student)
- Zoe Gidden (PhD Student)
- Alex Chappard (PhD Student)
Proteins are vital macromolecules within all cells; however, they rarely act alone. Most of the processes that occur within cells are carried out by molecular machines that are composed of a myriad of protein constituents, held together by both covalent and non-covalent interactions. Our understanding of how proteins work has been fed by a wide variety of powerful biochemical, structural, and genetic approaches. These methods, however, traditionally rely on averaging a signal over a large ensemble of protein molecules, obscuring important kinetic details, and preventing the detection of rare species. Our group develops and uses single-molecule and super-resolution microscopy approaches to detect and characterise individual molecules below the diffraction-limit of light in the test-tube, cells and tissue.
Our group is interested in applying single-molecule and super-resolution microscopy techniques to answer a range of biological questions. We have a focus on neuroscience and neurodegenerative diseases, but also work on other projects, including those related to cardiovascular diseases.
Despite having different clinical characteristics, many neurodegenerative disorders, such as Alzheimer’s and Parkinson’s disease are similar at the molecular level. Both are part of a growing family of protein misfolding diseases that have radically different causes than other disorders. In such diseases, individual proteins aggregate to form oligomers, which then go on to form large fibrillar deposits. It is now recognised that the amyloid oligomers are the main pathogenic species. These, however, are notoriously difficult to study using classical analytical methods, as they are highly heterogeneous and rare relative to the monomeric protein. Single-molecule approaches allow the rare populations of oligomers to be characterised in high detail.
Mathew was born and brought up in Halifax, West Yorkshire, before studying Chemistry at Oriel College, University of Oxford. He did his Master's project with Professor Mark Wallace, where he was first introduced to single-molecule techniques. Following this, he moved to the University of Cambridge to work with Professor Sir David Klenerman, developing microscopy techniques to study the protein aggregates formed in neurodegenerative disorders, such as Parkinson’s and Alzheimer’s disease.
Following a brief stint researching in New South Wales, Australia, Mathew returned to Cambridge in 2016 to take up a Junior Research Fellowship at Christ’s College, and a Herchel Smith Fellowship at the University of Cambridge. He moved to the University of Edinburgh to head the ESMB Group in January 2018. He was the 2022 winner of the Royal Society of Chemistry’s Joseph Black award.
When not in the lab, Mathew enjoys competing in triathlons, and has completed an Ironman in Weymouth (2016).
UCB Biopharma (Industry)
Medical Research Scotland
Honours and Awards
Royal Society of Chemistry Joseph Black Award for Analytical Chemistry (2022)