Journal article

Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide

Emily H Pilkington, Ove JR Gustafsson, Yanting Xing, Juan Hernandez-Fernaud, Cleidi Zampronio, Aleksandr Kakinen, Ava Faridi, Feng Ding, Paul Wilson, Pu Chun Ke, Thomas P Davis

ACS Nano | American Chemical Society | Published : 2018

Abstract

Amyloids may be regarded as native nanomaterials that form in the presence of complex protein mixtures. By drawing an analogy with the physicochemical properties of nanoparticles in biological fluids, we hypothesized that amyloids should form a protein corona in vivo that would imbue the underlying amyloid with a modified biological identity. To explore this hypothesis, we characterized the protein corona of human islet amyloid polypeptide (IAPP) fibrils in fetal bovine serum using two complementary methodologies developed herein: quartz crystal microbalance and “centrifugal capture”, coupled with nanoliquid chromatography tandem mass spectroscopy. Clear evidence for a significant protein co..

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University of Melbourne Researchers

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Awarded by ARC Project


Awarded by NSF CAREER CBET


Awarded by NIH MIRA


Awarded by Leverhulme Trust


Awarded by NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES


Funding Acknowledgements

This work was supported by ARC Project CE140100036 (to T.P.D.), NSF CAREER CBET 1553945 (to F.D.), and NIH MIRA R3SGM119691 (to F.D.). T.P.D. is thankful for an ARC Australian Laureate Fellowship. P.W. acknowledges a fellowship from the Leverhulme Trust (ECF/2015-075). E.H.P. acknowledges the support of an Australian Government RTP scholarship. TEM imaging was undertaken at the Bio21 Advanced Microscopy Facility. HIM imaging was performed at the UniMelb MCFP platform by B. Nasr. Mass spectrometry was undertaken at the Warwick Proteomics Research Technology Platform (UK).