Amyloid Proteins in Medullary Thyroid Cancer and Laryngeal Amyloidosis
Research type
Research Study
Full title
An ex vivo study to purify amyloid fibrils and solve their 3D structures using amyloid proteins from medullary thyroid cancer and laryngeal amyloidosis
IRAS ID
289680
Contact name
James Moor
Contact email
Sponsor organisation
Leeds Teaching Hosptials NHS Trust
Duration of Study in the UK
3 years, 0 months, 1 days
Research summary
The study aims to work out the 3-dimensional structure of proteins called amyloid, or more specifically, a part of the protein called the 'fibrils'. Amyloid proteins and their fibrils are formed in patients when certain types of proteins glue themselves together in specific circumstances, and can contribute to the development of some diseases. We believe that if we can understand the 3D structures of amyloid proteins and amyloid fibrils we will then be able to develop experiments that aim to;
1) understand whether specific problems with a patient's genes (called gene mutations) can increase the likelihood of a patient developing a disease related to amyloid proteins and amyloid fibrils
2) understand whether amyloid proteins undergo changes in their shape and structure (called post-translational modification) which also links to development of amyloid-related diseases
3) help in the development of new molecules that may influence the amyloid proteins becoming stuck together (this would potentially be the first step in the future development of a medical treatment for amyloid-related disease).REC name
HSC REC B
REC reference
21/NI/0026
Date of REC Opinion
26 Jan 2021
REC opinion
Favourable Opinion