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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