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David Allsop supervises 6 postgraduate research students. If these students have produced research profiles, these are listed below:

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Professor David Allsop

Professor

David Allsop

Lancaster University

Furness Building

LA1 4YG

Lancaster

Tel: +44 1524 592122

Research overview

I am interested in the pathological role of misfolded 'amyloid' proteins in a range of different human diseases, including some important neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease, and also late-onset diabetes.

My research is concerned with the mechanism of formation and deposition of these protein aggregates, the relationship between protein aggregation and tissue damage, and in novel approaches to diagnosis and therapy.

PhD supervision

PhD projects are available in all of the following areas of research:
1. Mechanism of amyloid toxicity
2. Disease-linked proteins as potential biomarkers
3. Amyloid inhibitors as novel therapeutics

Current Research

Current projects in my laboratory include:

  • Further development of retro-inverted peptides and peptide-inhibitor-nanoparticles as β-amyloid aggregation inhibitors, for the treatment of Alzheimer's disease. This is the project of PhD student Maria Michael and has been supported by EU, Alzheimer's Research UK and The Alzheimer's Society.
  • Development of peptide-based inhibitors of amylin aggregation for the treatment of late-onset (type 2) diabetes. This is the project of PhD student Idira Obasse and is partly supported by a Faculty of Health and Medicine Doctoral Studentship. Idira has just submitted her PhD.
  • Establishment of a multiplex luminex-bead immunoassay system for the early diagnosis of neurodegenerative diseases. This work is supported by an equipment grant from Alzheimer's Research, UK and by grants from The Eleanor Peel Foundation, The Joy Welch Trust and Open Innovation Challenge for Neurodegenerative Diseases, and is a collaboration with Prof. David Mann from University of Manchester. This is the project of Kurimun Ismail who has just completed her PhD.
  • Recent research in collaboration with Professor Barbara Maher (LEC) has identified, for the first time, the presence of pollution-derived magnetite nanoparticles in the human brain. We are now investigating the toxic effects of these particles on cultured brain cells (project of PhD Student Jessica Hammond).

Research Interests

The formation of fibrillar aggregates is a common feature of numerous different 'protein conformational' diseases. In these diseases, normally soluble proteins are deposited in the form of insoluble fibrils inside and/or outside of cells. In the systemic amyloidoses, extracellular fibrillar deposits (often called amyloid) can be found in many different tissues and organs throughout the body. Localised deposits are found in some other diseases, such as late-onset diabetes, where they are restricted to the pancreas, and some important neurodegenerative diseases, where they are found in the brain and central nervous system. Examples of the latter include Alzheimer's disease, Parkinson's disease, the prion diseases (e.g. CJD), Huntington's disease, frontotemporal dementia and motor neuron disease. My research is concerned with the pathological role of these misfolded proteins.

Research Interests

There are three major aspects to my research:

1. Mechanism of amyloid toxicity

We are studying the potential mechanisms by which the accumulation of protein aggregates can lead to cellular degeneration and loss and have discovered that the aggregating proteins implicated in Alzheimer's disease, Parkinson's disease, prion disease and late-onset diabetes all have the common ability to generate hydrogen peroxide and hydroxyl free radicals. They appear to do this through key interactions with redox-active transition metal ions, particularly iron and copper. Our current hypothesis is that tissue damage caused by the formation of 'reactive oxygen species' could be a common mechanism of cell damage in several different protein misfolding disorders.

2. Disease-linked proteins as potential biomarkers

A further aspect of our research is the detection of proteins implicated in the pathogenesis of neurodegenerative disease as potential biomarkers in body fluids (cerebrospinal fluid and blood). There are two main aspects to this work:

  • The development of improved diagnostic markers, to allow early detection and consequently improved treatment of disease.
  • The development of molecular markers to enable the tracking of disease progression in already diagnosed patients - this would help to streamline drug testing in clinical trials.

Our current research in this area is focussed on markers for Parkinson's disease. Recently, we carried out the first longitudinal study on α-synuclein as a biomarker for Parkinson's disease (supported by MRC) and are now developing a 'multiplex bead' assay system for simultaneous determination of multiple biomarkers.

3. Amyloid inhibitors as novel therapeutics

Blocking the formation of early toxic protein aggregates could be a novel approach to the treatment of protein misfolding diseases. We have recently developed a retro-inverted peptide aggregation inhibitor that could provide a new treatment for Alzheimer's disease, and are following a similar strategy for late-onset diabetes. We have also found that the potency of these inhibitors can be greatly improved by attaching them to nanoparticles. We are also studying some novel glycopeptidomimetics and β-Hairpin mimics made by chemists in France (Paris-SUD).

Our Research has been supported by grants from Medical Research Council, Engineering and Physical Sciences Research Council, European Union, The Wellcome Trust, Alzheimer's Society, Alzheimer's Research UK and The Sir John Fisher Foundation.

Total grant income over the last ten years has exceeded £2.4 million.

Current Teaching

BIOL125: HUMAN PHYSIOLOGY (Module Organiser), 12 lectures on the nervous system, cardiovascular system, lungs and respiration, and the digestive system; 8 practical classes/workshops

BIOL354: PATHOBIOLOGY (Module Organiser), 3 lectures on brain diseases; 5 practicals/workshops

BIOL364: AGEING, 1 lecture on the ageing brain

 

Additional Information

  • Member of Research Executive Committee, The Alzheimer's Society  
  • Member of Editorial Board of the International Journal of Alzheimer's Disease

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