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Dr Wei-Feng Xue

Senior Lecturer in Chemical Biology

School of Biosciences


List of selected recent publications, view full publication list on Google Scholar or in the Kent Academic Repository

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? This is a question of fundamental biological importance, and the focus of the research in my lab.

Amyloid fibrils are highly ordered protein assemblies with the cross-beta structure consisting of continuous beta-sheets running through the core of amyloid fibrils perpendicularly to the fibril axis. Not all amyloid assemblies are associated with disease as some have been recognised as functional amyloids that can play a number of important roles in organisms ranging from bacteria and yeast to humans. My research interests and expertise are in structural biology, biochemistry, chemical biology, biophysics and computational biology of protein assembly, protein folding, protein misfolding, amyloid and prions. My research is focused on resolving the lifecycle of amyloid protein assembly using experimental, computational and theoretical approaches, including AFM/EM imaging, spectroscopy, kinetics, recombinant protein production, yeast molecular biology and cell biology methods.

Dr Wei-Feng Xue joined the school of Biosciences in 2011 as Lecturer in Chemical biology, and he is now Senior Lecturer in Chemical biology since 2014. He received his PhD degree in Physical Chemistry on research regarding protein-protein/protein-ligand interactions in Prof. Sara Linse's group at Lund University in Sweden (2006). He then went on to do postdoctoral research concerning the mechanism and the biological impact of amyloid assembly in Prof. Sheena Radford's laboratory at the Astbury Centre for Structural Molecular Biology in the University of Leeds (2006-2011). His research interests include supramolecular protein assembly, protein folding and misfolding, amyloid and prions, and AFM imaging.

Wei-Feng is a member of the Kent Fungal Group, the Protein Form and Function Group and the Industrial Biotechnology Centre

ORCID ID: 0000-0002-6504-0404

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Also view these in the Kent Academic Repository

Marchante, R. et al. (2017). The physical dimensions of amyloid aggregates control their infective potential as prion particles. eLife [Online] 6:e27109. Available at:
Al-Hilaly, Y. et al. (2016). The involvement of dityrosine crosslinking in α-synuclein assembly and deposition in Lewy Bodies in Parkinson's disease. Scientific Reports [Online] 6:39171. Available at:
Miller, C. et al. (2016). A new platform that enables long-term cultivation of Cryptosporidium. Scientific Reports.
Eugène, S. et al. (2016). Insights into the variability of nucleated amyloid polymerization by a minimalistic model of stochastic protein assembly. The Journal of Chemical Physics [Online] 144:175101. Available at:
Mayer, M. et al. (2016). Effect of bio-engineering on size, shape, composition and rigidity of bacterial microcompartments. Scientific Reports [Online] 6:36899. Available at:
Smith, R. et al. (2015). Analysis of Toxic Amyloid Fibril Interactions at Natively Derived Membranes by Ellipsometry. PLOS ONE [Online] 10:e0132309. Available at:
Xue, W. (2015). Nucleation: The Birth of a New Protein Phase. Biophysical Journal [Online] 109:1999-2000. Available at:
Marshall, K. et al. (2014). The relationship between amyloid structure and cytotoxicity. Prion [Online] 8:192-196. Available at:
Jakhria, T. et al. (2014). Beta2-Microglobulin Amyloid Fibrils Are Nanoparticles That Disrupt Lysosomal Membrane Protein Trafficking and Inhibit Protein Degradation by Lysosomes. Journal of Biological Chemistry [Online] 289:35781-35794. Available at:
Tuite, M., Howard, M. and Xue, W. (2014). Dynamic Prions Revealed by Magic. Chemistry & Biology [Online] 21:172-173. Available at:
Lawrence, A. et al. (2014). Solution Structure of a Bacterial Microcompartment Targeting Peptide and Its Application in the Construction of an Ethanol Bioreactor. ACS Synthetic Biology [Online] 3:454-465. Available at:
Goodchild, S. et al. (2014). β2-Microglobulin Amyloid Fibril-Induced Membrane Disruption Is Enhanced by Endosomal Lipids and Acidic pH. PLoS One [Online] 9:e104492. Available at:
Sheynis, T. et al. (2013). Aggregation modulators interfere with membrane interactions of beta2-microglobulin fibrils. Biophysical Journal [Online] 105:745-755. Available at:
Xue, W. and Radford, S. (2013). An Imaging and Systems Modeling Approach to Fibril Breakage Enables Prediction of Amyloid Behavior. Biophysical Journal [Online] 105:2811-2819. Available at:
Milanesi, L. et al. (2012). Direct three-dimensional visualization of membrane disruption by amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America 109:20455-60.
Strawn, R. et al. (2011). Synergy of molecular dynamics and isothermal titration calorimetry in studies of allostery. Methods in Enzymology [Online] 492:151-88. Available at:
Xue, W. et al. (2010). Fibril fragmentation in amyloid assembly and cytotoxicity: When size matters. Prion [Online] 4:20-25. Available at:
Bauer, M., Xue, W. and Linse, S. (2009). Protein GB1 folding and assembly from structural elements. International Journal of Molecular Sciences [Online] 10:1552-1566. Available at:
Platt, G. et al. (2009). Probing Dynamics within Amyloid Fibrils Using a Novel Capping Method. Angewandte Chemie International Edition [Online] 48:5705-5707. Available at:
Xue, W. et al. (2009). Role of protein surface charge in monellin sweetness. Biochimica Et Biophysica Acta-Proteins and Proteomics [Online] 1794:410-420. Available at:
Xue, W. et al. (2009). Fibril Fragmentation Enhances Amyloid Cytotoxicity. Journal of Biological Chemistry [Online] 284:34272-34282. Available at:
Xue, W., Homans, S. and Radford, S. (2009). Amyloid fibril length distribution quantified by atomic force microscopy single-particle image analysis. Protein Engineering Design and Selection [Online] 22:489-496. Available at:
Xue, W., Homans, S. and Radford, S. (2008). Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly. Proceedings of the National Academy of Sciences of the United States of America [Online] 105:8926-8931. Available at:
Linse, S. et al. (2007). Nucleation of protein fibrillation by nanoparticles. Proceedings of the National Academy of Sciences of the United States of America [Online] 104:8691-8696. Available at:
Xue, W. et al. (2006). Intra- versus intermolecular interactions in monellin: contribution of surface charges to protein assembly. Journal of Molecular Biology [Online] 358:1244-1255. Available at:
Lindman, S. et al. (2006). Salting the charged surface: pH and salt dependence of protein G B1 stability. Biophysical Journal [Online] 90:2911-2921. Available at:
Jin, L. et al. (2005). Asymmetric allosteric activation of the symmetric ArgR hexamer. Journal of Molecular Biology [Online] 346:43-56. Available at:
Dell'Orco, D. et al. (2005). Electrostatic contributions to the kinetics and thermodynamics of protein assembly. Biophysical Journal [Online] 88:1991-2002. Available at:
Xue, W., Carey, J. and Linse, S. (2004). Multi-method global analysis of thermodynamics and kinetics in reconstitution of monellin. Proteins [Online] 57:586-95. Available at:
Showing 29 of 31 total publications in KAR. [See all in KAR]


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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.

Recombinant human alpha-synuclein amyloid fibrils imaged using atomic force microscopy (AFM)

Human alpha-synuclein  amyloid aggregates are found in Lewy Bodies associated with Parkinsons disease. The scale bar represents length of 100 nm.


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.


Key research themes of on-going projects in the Xue lab that involve fundamental research into the molecular mechanisms of amyloid formation


We are currently looking for enthusiastic and motivated students and postdoctoral researchers intent on securing own fellowships to join our lab. If you are interested in the research in my lab, please contact me by email: Following are some of the projects currently running in my lab:

What defines the seeding and cross-seeding potential of amyloid particles?

A number of devastating human brain disorders, for example Alzheimer's disease (AD), Hungtington's diseases, diabetes type 2 and transmissible spongiform emcephalopathies (TSEs), are associated with the abnormal folding of proteins. The net result of this misfolding is the formation of large insoluble protein deposits and small toxic protein particles in a state called amyloid. The deposition of aggregated protein material in various tissues (e.g. brain, liver etc) is one of the many common characteristics shared by these diseases. Importantly, these disorders also share a similar method by which the misfolded and aggregated proteins are propagated in the disease conditions. In this process, different proteins in the cell are triggered to undergo a major change in their structure to form the highly robust amyloid state. One crucial step in amyloid formation is that the addition of preformed amyloid particles, the seeds, can greatly accelerate amyloid growth, and this phenomenon is called seeding. In some cases these seed particles are considered as infectious entities, capable of transmitting the disease to neighbouring cells, tissues, or another individual of the same or a different species, as in the case of the TSEs and possibly in other amyloid diseases such as Alzheimer's disease. The current and projected impact of these diseases on human health and welfare cannot be understated yet the fundamental question of how is the amyloid state propagated through seeding remains to be fully resolved.
In some of the diseases associated with protein misfolding, more than one type of amyloid aggregate may exist where each type of aggregate is made of a protein with a different amino acid sequence. For example, in Alzheimer's disease the co- existence of various amyloid forms of the diagnostic amyloid-beta protein and at least one other different protein has been reported in patients including the presence of transmissible prion protein aggregates. Furthermore, recent reports have suggested that the onset of prion disease can be influenced and possibly enhanced by the presence of amyloid-beta deposits. This co-existence of two different amyloids in the same patient can be potentially explained by the interaction between misfolded proteins with each other, accelerating their respective conversions to the amyloid state. Therefore, the amyloid seeding and cross-seeding process is also potentially involved in the devastating synergetic effects in amyloid diseases.
Our aim is to study the fundamental process of amyloid seeding by a combination of test tube-based in vitro approaches as well as cell-based in vivo approaches using the baker's yeast Saccharomyces cerevisiae as a safe and experimentally tractable model. In our project we will map the seeding potency of well-characterised amyloid seed samples, monitoring the growth of the amyloid fibrils using natural seeds or seeds formed from other amyloid proteins, so called "cross-seeding". We will then investigate how "cross-seeding" occurs in the yeast cell using a novel yeast prion-based assay. Since yeast prions are infectious but non-toxic, this system allows us to follow amyloid formation and propagation without causing cell death and therefore we can investigate the fundamental principles of cross-seeding in a living cell. Overall, our project will allow us to establish the nature and spectrum of the potential interactions between misfolded proteins and the dependence, if any, on cellular components in generating this important disease-associated amyloid forms.

Collaborator: Prof. Mick Tuite, School of Biosciences (Kent). Funded by: BBSRC

Investigating the nano-scale properties of amyloid assembly

Detailed characterisation of amyloid fibrils of different origins has revealed incredibly strong structures that are commonly only tens of nanometres thick but many micrometres long. The unusual physical characteristics of amyloid fibrils mean that they have also the potential to become strong and stable engineered nanomaterials. Here, using atomic force microscopy imaging approach (AFM), we are investigating the physical and mechanical properties of in vitro formed amyloid fibrils.


Quantitative investigations into the molecular mechanisms of amyloid fibril fragmentation

Breaking amyloid fibrils into smaller pieces is a key process that must be fully understood if we are to understand how amyloid fibrils normally function in nature, and how they are involved in diseases so we can develop effective therapies against the amyloid-associated diseases and prion diseases. Fibril fragmentation is a key secondary process that accelerates amyloid assembly and enables prion propagation. The abilities of amyoid fibrils to seed the growth of new fibrils and to damage cells in disease has been linked to the length and the number of fibrillar aggregates present, which in-turn is related to their stability toward fragmentation. The long-term goal of this project is to resolve the molecular and cellular mechanisms of fibril fragmentation by investigating the breakage of amyloid fibrils, including fibrils formed from the yeast prion protein Sup35.
Collaborator: Prof. Mick Tuite, School of Biosciences (Kent). Funded by: BBSRC.


Understanding the nano-scale organisation of amyloid assembly by atomic force microscopy imaging

While the cross-β core molecular architecture of amyloid has been studied in detail, their long-range structural organisation in the nanometre to micrometre scale and how the long-rage structural properties relate to their disease association is not well known. In this project, we are examining the long-range structural organisation of amyloid fibrils formed in vitro from model peptides of short amyloidogenic sequences using quantitative atomic force microscopy (AFM) imaging.
Collaborator: Prof. Louise Serpell, School of Life Sciences, University of Sussex.

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  • First year
    BI321/BI3210: Biological Chemistry A (Module convenor)
    BI322/BI3220: Biological Chemistry B (Module convenor)
  • Third year
    BI600: Biology project
    BI629: Proteins: Structure and Function
  • MSc
    BI852: Advanced Analytical and Emerging Technologies for Biotechnology and Bioengineers
  • Summer student project coordinator
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We are currently looking for enthusiastic and motivated students and postdoctoral researchers intent on securing own fellowships. If you are interested in joining my group, please contact me by email:

Current lab members:
Postdoctoral Research Associates
Dr. Nadia Koloteva-Levine
Dr David Beal

Ph.D. Students
Ben Blakeman
Cassidy Mackenzie
Chloe Johnson

Tracey Purton


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Enquiries: Phone: +44 (0)1227 823743

School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ

Last Updated: 18/05/2017