University of Leeds
Andy Wilson- is interested in the development of inhibitors of protein-protein interactions, and using synthetic molecules to understand and control molecular recognition and self-assembly.
Adam Nelson- is currently exploiting small molecule libraries of exceptional scaffold diversity in the discovery of small molecular modulators of protein-protein interactions.
Stuart Warriner – has a strong record of collaboration to address major problems in cell biology (with Baker), protein folding (with Radford) and protein-ligand interactions (with Homans). Stuart has extensive experience in peptide chemistry and of developing and implementing large scale screens using plate and robotic technologies.
Paul Ko Ferrigno – identifies PPI inhibitors through a semi-rational process, whereby peptide aptamers are used to establish the PPI can be inhibited, and small molecules that are able to mediate the same effect are rationally identified, specifically the transcriptional co-repressor BCL-6.
Steve Homans – brings experience in the dynamics and thermodynamics of ligand protein-interactions. Through use of high-resolution NMR, isothermal titration calorimetry and computational methods to delineate the enthalpic and entropic contributions to binding from protein, ligand and solvent.
Thomas Edwards – uses a range of structural techniques particularly X-ray crystallography, NMR &complementary biophysical techniques to address key problems in cancer, cell and developmental biology including those involving PPIs.
Sheena Radford – uses an array of biophysical methods including NMR, mass spectrometry, single molecule methods to determine how proteins self-assemble e.g. into (a) fibrils associated with amyloid or (b) pili associatedwith bacterial colonization and infection. With a view to defining new routes towards intervention.
Alison Ashcroft – focuses on development and application of mass spectrometric-based methods to biological systems. Recent work has involved protein-protein interactions in amyloid assembly and in virus capsid assembly.
Alex Breeze- is interested in combining NMR spectroscopy with other structural and biophysical methods to interrogate both normal and disease biology at a molecular level, which involves using selective chemical biology probes.
Imperial College Institute of Chemical Biology
David Klug- is largely focussed on protein structure, function and dynamics. Major methods include the use of coherent two dimensional laser spectroscopy for proteomics, proteome-on-a-chip technology and microfluidic antibody capture chips for single cell proteomics.
Alan Armstrong- his research interests lie in synthetic organic chemistry and its application to biological problems. This includes protein-ligand engineering and the development of new chemical approaches for the discovery of inhibitors of protein-protein interactions.
Steve Matthews – Is head of the Imperial College Centre for Structural Biology and has an interest in the use of NMR for the study of PPIs.
Michael Stumpf – Is a systems biologist working on protein-protein networks, protein interactomes and a range of related problems.
Mike Sternberg – Director of the Centre for Bioinformatics. His groups main research interests are: Prediction of protein structure and function; Prediction of macromolecular docking and interactions; Network modelling for Systems Biology ; Logic-based drug design
Robin Leatherbarrow – Heads the Chemical Biology Section in the Department of Chemistry and has extensive track record enzyme inhibitors and rational design of peptide-based inhibitors.
Ed Tate – Specialises in chemical tools for the study of biological problems including activity based probes.
Ali Tavassoli (Southampton) – employs a genetic selection methodology that facilitates rapid screening of libraries of over a hundred million cyclic peptides (produced using SICLOPPS split-inteins in vivo) against a chosen PPI. His group use this methodology extensively for the selection of inhibitors of PPIs.
Rudolf Alleman (Cardiff) – has recently developed biophotonic nanoswitches that can be used to control reversibly through external light pulses the binding activity of the nanoswitches for DNA and RNA and through an EPSRC Basic Technology grant extended this approach to control PPIs in vitro and in vivo.
Nick Westwood (Eastchem St Andrews) – use high level methods in organic synthesis in the context of chemical biology and drug discovery projects. Recent work has involved the discovery and initial optimisation of the chemical tools blebbistatin, tenovin-6, tachyplegin and the conoidins.
Jim Naismith (Eastchem St Andrews) – brings experience in structural biology with particular strengths in protein production, the determination of structures of drug targets, the use of fragment-based screening approaches to identify starting point for inhibitor design and assay development.
Uli Schwarz-Linek (Eastchem St Andrews) – specialises in protein NMR and isothermal titration calorimetry to study protein interactions in solution. His group have developed these techniques as tools for small molecule binding and fragment screening (NMR).
Alison Hulme (Eastchem Edinburgh) – have developed a linker for affinity chromatography which is compatible with “click” chemistry, offering exciting new possibilities for target isolation and have an active collaboration with Profs Ball and Hupp at the Edinburgh Cancer Research Centre on the design of hDM2 inhibitors.
UCB (Martin Lowe) –is a biotech company with experience of developing small molecule and antibody-based therapeutics. They bring expertise in medicinal chemistry, protein engineering, x-ray crystallography and fragment screening technologies. UCB work on a number of PPI targets including VLA-4 (the development candidate from this, CDP-323, made it into phase II clinical trials) and BCL-2.
GSK (Mike Hann)- is a global pharmaceutical company with experience in researching and manufacturing innovative therapeutics. They are using protein crystallography, protein mass spectroscopy and biophysical methods to support their drug discovery activities.
Pfizer (David Pryde)- is a global biopharmaceutical company. Their exploratory team (based near Cambridge, UK) are responsible for advancing chemistry-led projects into the research unit in support of the Pfizer UK portfolio of pain and sensory disorder therapeutic targets.
Selcia (Bob Carling) – are using capillary electrophoresis (CE) as a screening methodology for the identification of fragment hits (small molecule weak binders) to proteins. CE is also applicable to study of PPI’s in targeted drug discovery (Pierceall, W.E., Zhang, L., and Hughes, D.E. (2004)).
Domainex – are a contract research organisation with significant interest in PPIs. They bring expertise in Medicinal Chemistry, Protein Expression, Structural Biology, Computational Chemistry and Biochemical Assays.
GE Healthcare – are a major international group that provide transformational medical and analytical technologies. With Biacore SPR and MicroCal Isothermal calorimetry they have 2 leading technologies for studying and characterising protein-protein and biomolecular interactions. In addition we will welcome the research councils and charities to the scientific meetings associated with the network and encourage the involvement of Learned Societies