Matt has a research background in molecular biology, particularly in protein DNA interaction. He is Head of School for Allied Health but still lectures in molecular biology and acts as External Examiner for a number of UK institutions.
Matt also serves on national bodies such as the Council of Deans for Health, and in 2019 was awarded Fellowship of the Royal Society of Biology for his work in scientific research and education.
Matt completed his undergraduate studies at the University of Kent before moving into industry. Having worked for a number of major pharmaceutical companies in the UK, he completed his PhD at the Institute of Structural and Molecular Biology under the supervision of Dr Tracey Barrett. Using the technique of Protein Crystallography he successfully solved the structure of the DNA damage repair protein UvRB, showing it to be dimeric in damage scanning.
Following postdoctoral work at Birkbeck College, Matt secured a research fellowship with Cancer Research UK, working in the laboratory of Dr Martin Singleton and investigating the role of various Histone binding proteins in the formation of the mitotic spindle.
Matt has always had a keen passion for science education and moved to a post at ARU's associate college in Harlow where he led the validation and delivery of a new BSc (Hons) in BioScience. Following roles within the main institution Matt has led the School of Allied Health since 2018 and overseen its rise to being a leading provider of clinical and non-clinical provision to the Eastern and London regions.
Suliman, A. S., Khoder, M., Tolaymat, I., Webster, M., Alany, R. G., Wang, W., Elhissi, A., Najlah, M., 2020. Cyclodextrin Diethyldithiocarbamate Copper II Inclusion Complexes: A Promising Chemotherapeutic Delivery System against Chemoresistant Triple Negative Breast Cancer Cell Lines. Pharmacuetics, 13(1): p. 89.
Webster, M., 2020. Coronavirus mutation - not as scary as it sounds. The Conversation.
Webster, M. P., Jukes, R., Zamfir, V. S., Kay, C. W., Bagnéris, C., Barrett T., 2012. Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes. Nucleic Acids Research, 17(40), pp. 8743-58