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Inhibiting protein-protein interactions in the early stages of amyloid formation

Project Description

Amyloidosis is a pathological condition associated with the aggregation of proteins into fibrils. Despite the importance of amyloid diseases in today’s society, therapies remain remote, due to a lack of understanding of some of the fundamental molecular processes involved.
In this project we will use directed evolution, biochemistry, native mass spectrometry and other biophysical assays, to develop new inhibitors of amyloid formation and to determine their mechanism of action in structural detail. In parallel, cell biology will be used to determine whether ligands that bind the proteins of interest also inhibit cytotoxicity. The project will focus on amylin (IAPP), involved in type II diabetes, and A involved in Alzheimer’s disease, two of the major diseases challenging today’s society and for which there are currently no effective therapeutics on the market.

The student employed will learn a variety of skills in this multi-disciplinary project that, together, will open the door to new understandings of how and why amyloid fibril formation kills cells and whether small molecules can ameliorate or even inhibit this deadly process.

Funding Notes

White Rose BBSRC Doctoral Training Partnership in Mechanistic Biology
4 year fully-funded programme of integrated research and skills training, starting Oct 2019:
• Research Council Stipend
• UK/EU Tuition Fees
• Conference allowance
• Research Costs

At least a 2:1 honours degree or equivalent. We welcome students with backgrounds in biological, chemical or physical sciences, or mathematical backgrounds with an interest in biological questions.
EU candidates require 3 years of UK residency in order to receive full studentship

Not all projects advertised will be funded; the DTP will appoint a limited number of candidates via a competitive process.

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Related Subjects

How good is research at University of Leeds in Biological Sciences?

FTE Category A staff submitted: 60.90

Research output data provided by the Research Excellence Framework (REF)

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