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Understanding the Structure, Toxicity and Inhibition of IAPP at the Nanoscale

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posted on 01.06.2020 by EMILY HELEN PILKINGTON
Aggregation of human islet amyloid polypeptide (IAPP) to form amyloid fibrils and plaques is implicated in the dysfunction and death of pancreatic beta cells in type 2 diabetes, a most common form of metabolic disease. Accordingly, this thesis investigated the amyloidosis of IAPP, its self-assembly into toxic aggregation states, and its interactions with proteins and lipids to acquire a ‘protein corona’, a concept pertinent to the targeting of a range of amyloid diseases. Advised by this knowledge, a star polymer was then synthesised to successfully protect pancreatic beta cells and islets from IAPP-mediated toxicity through hydrophobic interaction and hydrogen bonding.

History

Campus location

Australia

Principal supervisor

Pu-chun Ke

Additional supervisor 1

Paul Wilson

Additional supervisor 2

Thomas Davis

Year of Award

2020

Department, School or Centre

Drug Delivery, Disposition and Dynamics

Additional Institution or Organisation

University of Warwick

Course

Doctor of Philosophy (Joint PhD with The University of Warwick)

Degree Type

DOCTORATE

Exports

Exports