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Lab move

As part of a major refurbishment of the Faculty of Biological Sciences, the Jeuken Group will move into a new (temporary) location. The move will start on 16 June.

A simple way to make multilayer lipid membranes

Multilayer lipid membranes form many important functions in biology and various biomimetic multilayer membranes have been reported in literature. However, all of these biomimetic systems suffer from long preparation times, speciality chemicals and/or irreproducibility problems between different labs. George Heath developed a very simple multilayer model membrane system that is based on layer-by-layer assembly of poly-L-lysine and lipid membranes.DOI: 10.1021/acs.biomac.5b01434

Unexpected high H2O2 reduction activity of a decaheme protein for applications in fuel cells.

Congratulations to our collaborators in Cambridge, Dr. Bernard Reuillard, who works with Dr. Erwin Reisner in Chemistry. He found an unexpected fast electrocatalytic reduction of H2O2 when he modified ITO electrodes with a decaheme protein, MtrC. Although MtrC showed lower peroxidase activity in solution compared to horseradish peroxidase, the ten heme cofactors enable excellent electronic communication with ITO and, as a result, displayed a superior activity on the electrode surface.DOI: 10.1021/jacs.6b12437


Our aim is to to control the interaction between biological macromolecules and inorganic 'solid' surfaces. The interaction between biomolecules and surfaces is key to many assays, but often not controlled. Take for instance an ELISA assay; Biomolecules are 'randomly' physisorbed on plastic 96-well plates without any control on the orientation of these molecules. However, biomolecules for which the epitope is orientated towards the plastic surfaces might not interact with antibodies. The interaction between solid, inorganic surfaces is particular important for membrane proteins, where the hydrophobic regions of the protein will change the way the proteins interacts with its environment. Vice versa, the influence of inorganic surfaces on proteins might be more pronounces for membrane proteins, denaturing the protein or otherwise influencing the function of the membrane proteins. Membrane proteins, in general, are more difficult to study due to their amphiphatic nature. Many membrane enzymes are studied in detergent solutions or only hydrophilic subunits are used (i.e., removing the integral membrane subunits). However, the lipid membrane has an important influence on the proteins that reside in them and experimental techniques that do not include the membrane are thus limited. When studying membrane proteins with assays that include their adsorption to a solid surface, one would ideally like to retain a native-like lipid environment. Important examples are enzymes that interact with the hydrophobic quinone pool (like ubiquinol oxidase). Other examples include 'membrane-bound hydrogenases', where the majority of studies are performed on the two hydrophilic subunits, without the third transmembrane quinone-converting subunit.

In our group, we chemical modify surfaces with the aim to control the interaction between membrane proteins (or whole membranes) and the surface. We call these modifications ''membrane-modified surfaces'. Our surfaces are characterised with a broad spectrum of tools, including Quartz-Crystal Microballance with Dissipation (QCM-D) and Atomic Force Spectroscopy (AFM). We are extending our research into controlling the interaction between solid surfaces (including nanoparticles) and whole bacteria, which has important applications in microbial electrochemistry.

The interaction between (membrane) proteins and inorganic surfaces is also important in 'nanotoxicology'. Nanotoxicology is a field where we study and determine possible toxic effects that nanoparticles might have and importantly, how these effects differ from the same material in the macroscopic form.

For more information about our research and projects, please press the 'research' or ERC 'MEME' tab on the top-left of this page.

Due to the interdisciplinary nature of our research, we are a connected to a number of school and centres in Leeds

  • School of Biomedical Sciences (SBMS) of the Faculty of Biological Sciences
  • Molecular and Nano-Partical group (MNP) within the School of Physics & Astronomy
  • Astbury Centre and the Institute for Molecular Biophysics (Astbury)



Lars J. C. Jeuken
School of Biomedical Sciences
Leeds LS2 9JT UK
+44 (0)113 - 3433829
Office: Garstang (Bioincubator), 7.31