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Home > Research > Researchers > David Allsop
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David Allsop supervises 6 postgraduate research students. Some of the students have produced research profiles, these are listed below:

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Professor David Allsop

Professor

David Allsop

Furness Building

Lancaster University

Bailrigg

Lancaster LA1 4YG

United Kingdom

Tel: +44 1524 592122

Location:

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 is a collaboration with Prof. Christian Hölscher at Lancaster University. This work has been supported by EU and Alzheimer's Research UK.
  • 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.
  • Establishment of a mutiplex 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 and The Joy Welch Trust and is a collaboration with Prof. David Mann from University of Manchester. This is the project of PhD student Kurimun Ismail.
  • Development of α-synuclein as a diagnostic marker to distinguish between Alzheimer's disease and Lewy body dementia. This project is being carried out by Dr. Mark Taylor and Kurimun Ismail and is funded by an Alzheimer's Research UK Centre Co-operation Grant involving Lancaster, Manchester and Newcastle Universities.
  • Understanding of the role of metal ions and oxidative damage in toxicity of the β-amyloid protein found in Alzheimer's disease. This work is being carried out by Dr. Jennifer Mayes and is funded by The Sir John Fisher Foundation.
  • Use of sophisticated scanning probe microscopy techniques for detection of different stages of aggregation and for monitoring the effects of inhibitors (collaboration with Oleg Kolosov from Physics) - this is the PhD project of Claire Tinker, and is supported by EPSRC    

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 in humans), 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 radicals. They appear to do this through key interactions with redox-active transition metal ions, particularly 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 Aβ, tau, α-synuclein, TDP-43, LRRK2 and parkin. We were the first research group to detect the presence of some of these proteins in human blood plasma. 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 related to neurodegenerative disease.

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 novel retro-inverted peptide-based aggregation inhibitor that could provide a new treatment for Alzheimer's disease, and we are following a siimilar strategy for late-onset diabetes. We have also found that the potency of these inhibitors can be greatly improved by attaching them to nanoparticles.

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, The Sir John Fisher Foundation, Eleanor Peel Trust, George Barton Trust and Joy Welch Trust. 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

BIOL332: NEUROBIOLOGY, 3 lectures on development of the brain and nervous system

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

BIOL364: AGEING, 1 lecture on the ageing brain

BIOL436: BRAIN DISEASES (Module Organiser), 4 lectures on protein misfolding and brain diseases; 2 workshops on amyloid and reactive oxygen species

 

Additional Information

  • Member of Steering Committee for DeNDRoN North West
  • Regular Member and Chair of Grant Awarding Panel, The Alzheimer's Society
  • 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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