Understanding the Structure, Toxicity and Inhibition of IAPP at the Nanoscale
thesisposted on 01.06.2020 by EMILY HELEN PILKINGTON
In order to distinguish essays and pre-prints from academic theses, we have a separate category. These are often much longer text based documents than a paper.
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.