Portrait of Dr Wei-Feng Xue

Dr Wei-Feng Xue

Reader in Chemical Biology
Director of Biochemistry Programme


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 

ORCID: orcid.org/0000-0002-6504-0404

Research interests

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
First year 

  • BI321/BI3210: Biological Chemistry A (Module convenor) 
  • BI322/BI3220: Biological Chemistry B (Module convenor) 

Second year 

  • BI520: Metabolism and Metabolic Disease 
  • BI532: Skills for Bioscientists 2 

Third year 

  • 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: w.f.xue@kent.ac.uk potential project titles and descriptions are listed below,
Please note all projects will incur additional research costs of £1500.

Integrative atomic force microscopy for structural analysis of bio-molecules 
It has been more than 30 years ago since Gerd Binnig and Heinrich Rohrer shared half of the Nobel prize in physics (the predecessor of AFM) with Ernst Ruska for invention of electron microscopy in 1986. Cryo-electron microscopy (Cryo-EM) has since then revolutionised structural biology studies of bio-molecules (Nobel prize in Chemistry in 2017). This project will bring together AFM and Cryo-EM methods and develop new integrated methodologies that allow the visualisation of individual molecules. This project will involve computational analysis of cryo-EM maps using state of the art AFM analysis methods developed in the Xue lab. A key area to be investigated will be to compare AFM images of recombinant SARS-CoV 2 Spike protein collected in the Xue lab with structural information available in databases in an effort to contribute to the ongoing research in the school on the COVID-19 pandemic. This project can be carried out through remote working. 

Structural biology of amyloid aggregates
A number of human disorders, for example Alzheimer’s disease (AD), Parkinson's disease (PD), type 2 diabetes, and transmissible spongiform emcephalopathies (TSEs), are associated with the abnormal folding and assembly of proteins. The net result of this misfolding is the formation of large insoluble protein deposits and small toxic and possibly transmissible protein particles in a state called amyloid. Amyloid diseases account for increasing medical and social importance, for example, more than half million people are suffering from AD in the UK alone, and PD affects about 1% of the population over the age of 60. The aim of this project is to identify and understand the structural organisation and structural polymorphism of amyloid aggregates using nano-scale imaging methods that includes atomic force microscopy (AFM) and electron microscopy (EM). 

Synthetic biology approach to self-assembled fibrous bio-materials
The aims for this project is to design and produce functional amyloid fibrils displaying a specific structural organisation or a selection of enzymes or small molecule/metal binding motifs, and to evaluate the structure and of these fibrils using cutting-edge AFM imaging analysis, as well as the designed function of these fibrils in vitro or in vivo in cells.

Computational structural biology of filamentous disease associated amyloid assemblies
The aim of this project is to identify and understand the structural organisation of amyloid aggregates using nano-scale imaging methods. In this computational project, AFM image data will be analysed using state of the art 3D reconstruction methods developed in the Xue lab to characterise and compare the molecular structures involved in the formation, growth and the division of amyloid aggregates grown from disease associated amyloidogenic proteins. There will also be opportunities to learn aspects of computer coding and data analysis algorithm development. This project can be carried out through remote working.


  • Editorial Board Member: Scientific Reports 
  • Editorial Board Member: Frontiers in Molecular Biosciences
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