Journal article

Lysophosphatidylcholine modulates the aggregation of human islet amyloid polypeptide

Yanting Xing, Emily H Pilkington, Miaoyi Wang, Cameron J Nowell, Aleksandr Kakinen, Yunxiang Sun, Bo Wang, Thomas P Davis, Feng Ding, Pu Chun Ke

Physical Chemistry Chemical Physics | ROYAL SOC CHEMISTRY | Published : 2017


Amyloid aggregation of human islet amyloid polypeptide (IAPP) is a hallmark of type 2 diabetes (T2D), a metabolic disease and a global epidemic. Although IAPP is synthesized in pancreatic β-cells, its fibrils and plaques are found in the extracellular space indicating a causative transmembrane process. Numerous biophysical studies have revealed that cell membranes as well as model lipid vesicles promote the aggregation of amyloid-β (associated with Alzheimer's), α-synuclein (associated with Parkinson's) and IAPP, through electrostatic and hydrophobic interactions between the proteins/peptides and lipid membranes. Using a thioflavin T kinetic assay, transmission electron microscopy, circular ..

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Awarded by ARC

Awarded by NSF CAREER

Awarded by NIH MIRA

Funding Acknowledgements

This work was supported by ARC Project CE140100036 (Davis), NSF CAREER CBET-1553945 (Ding), NIH MIRA R35GM119691 (Ding) and Monash Institute of Pharmaceutical Sciences (Ke). Davis is thankful for the award of an ARC Australian Laureate Fellowship. Pilkington acknowledges an Australian Government Research Training Program (RTP) Scholarship.