Dr Wei-Feng Xue
What are the mechanisms that govern the formation of amyloid protein structures associated with human diseases such as Alzheimer’s disease, Parkinson’s disease, type 2 diabetes, Prion diseases and systemic amyloidosis? Why are some amyloid associated with devastating diseases while others are tolerated by cells or even perform functions important for life? These questions of fundamental biological importance are the focus of the research in the Xue laboratory.
Dr Wei-Feng Xue joined the school of Biosciences in 2011. He received his PhD degree in Physical Chemistry on research regarding protein-protein, protein-ligand and allosteric interactions in Prof. Sara Linse’s group at Lund University in Sweden in 2006. He then went on to become a postdoctoral fellow in the laboratory of Prof. Sheena Radford FRS at the Astbury Centre for Structural Molecular Biology at the University of Leeds on research topics concerning the mechanism and the biological impact of amyloid assembly. His research interests include supramolecular protein assembly, protein folding and misfolding, amyloid and prions, and AFM imaging.
Dr Wei-Feng Xue is a member of the Kent Fungal Group, and the Industrial Biotechnology Centre
Amyloid structures consist of highly ordered forms of protein assembled from whole or parts of normal soluble proteins or peptides of diverse amino acid sequences. The devastating human diseases associated with amyloid, such as Alzheimer's disease, Creutzfeldt-Jakob (CJD prion disease), Huntington's disease, Parkinson disease, type II diabetes mellitus, and systemic amyloidosis, are linked to the way the amyloid structures are assembled and deposited in the brain or in other parts of the human body. But far from all amyloid assemblies are disease-associated, as some amyloid fibrils have also been recognised as a class of functional protein assemblies, which can play a number of important roles in bacteria, yeast and humans. A sub-class of amyloid can spread between organisms by forming small seeds through the breakage of larger fibrils. These are called prions, and they exist in humans where they cause prion diseases such as CJD. In yeast, prions confer special cellular properties in yeast cells that are passed on from generation to generation, as a form of epigenetic or 'protein gene'. Amyloid fibrils are defined by their cross-beta core structure, where continuous beta-sheets run through the core of amyloid fibrils perpendicularly to the fibril axis.
My research is focused on resolving the fundamental mechanisms that govern the formation and the molecular lifecycle of amyloid protein aggregates. The long-term research vision in my lab is to fully understand the assembly of protein fibrils, as well as how different mechanisms involved in amyloid assembly are linked to the disease-associated properties and useful biological functions of amyloid.
Programme director for Biochemistry
- BI321/BI3210: Biological Chemistry A (Module convenor)
- BI322/BI3220: Biological Chemistry B (Module convenor)
- BI520: Metabolism and Metabolic Disease
- BI532: Skills for Bioscientists 2
- BI600: Biology project
- BI629: Proteins: Structure and Function
- BI852: Advanced Analytical and Emerging Technologies for Biotechnology and Bioengineers MSc by Research projects
We are currently looking for enthusiastic and motivated postgraduate students (MSc by research and PhD) as well as postdoctoral researchers intent on securing own fellowships to join our lab. If you are interested in the research in my lab, please contact: email@example.com potential project titles and descriptions are listed below,
Please note all projects will incur additional research costs of £1500.
- Editorial Board Member: Scientific Reports
- Editorial Board Member: Frontiers in Molecular Biosciences