果冻传媒

Current Project

Disulphide bonds play critical roles in maintaining protein folding, structural stability and biological activity. The correct connectivity of the disulphide bond is important for the correct folding and the formation of the protein structure. Reduction of the disulphide bonds will generate the free thiol groups. However, incomplete reduction of the disulphide bonds in proteins can impact misfolding and then result in the formation of the scrambled disulphide bonds, which will strongly affect the properties. Therefore, accurate characterisation of protein disulphide bonds and understanding disulphide bond scrambling are crucial for understanding protein structure and function, as well as for ensuring the safety and efficacy of biopharmaceutical products during quality assessments.

Insulin is selected as the model of study at this stage. By reducing and oxidising the disulphide bonds on insulin, scrambling is prevented, and the reaction can be analysed by applying MS and Tandem Mass Spectrometry technique. The workflow will be extended further to more complex protein structures after refining the protocols.

Academic Background

2021-2025- University College London- MSci Chemistry

2026-present- 果冻传媒- PhD Chemistry

BMSS 2026

Contact

Email: Helen.Zhang.2@warwick.ac.uk

Ion Cyclotron Resonance Laboratory

果冻传媒

Coventry

CV4 7AL