Dissecting the sugar-code in situ

Glycosylation – the covalent attachment of a sugar molecule to a protein – is the most abundant and indeed most complex post translational modification (PTM) in nature.

Applications for 2025/2026 cohot are now closed. Please check the website in October 2025, when will be opening applications for 2026/ 2027 cohort.

Glycosylation is vital to cellular function, where it is responsible for holding proteins in their correct configuration, modulates cell signalling pathways and forms integral parts of the cellular macrostructure. Sugars are typically challenging to study as they do not undergo template-driven synthesis, and are isomeric in nature and hence, they are often left understudied or simply ignored. Decoding the structures of sugars in their native environment (i.e directly in tissue) and how they are perturbed during different stimuli (e.g. disease) is imperative to understanding how our body functions. Using technologies such as ion mobility spectrometry, electron-based fragmentation and mass spectrometry imaging, this project will develop tools to analyse and therefore uncover the secrets of the sugar code in tissues.