Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide

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

Research output: Contribution to journalArticleResearchpeer-review

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 corona was obtained. No trends were identified for amyloid corona proteins based on their physicochemical properties, whereas strong binding with IAPP fibrils occurred for linear proteins or multidomain proteins with structural plasticity. Proteomic analysis identified amyloid-enriched proteins that are known to play significant roles in mediating cellular machinery and processing, potentially leading to pathological outcomes and therapeutic targets.

Original languageEnglish
Pages (from-to)6066-6078
Number of pages13
JournalACS Nano
Volume12
Issue number6
DOIs
Publication statusPublished - 26 Jun 2018

Keywords

  • amyloid
  • amyloidogenesis
  • liquid chromatography
  • mass spectrometry
  • protein corona

Cite this

Pilkington, E. H., Gustafsson, O. J. R., Xing, Y., Hernandez-Fernaud, J., Zampronio, C., Kakinen, A., ... Davis, T. P. (2018). Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide. ACS Nano, 12(6), 6066-6078. https://doi.org/10.1021/acsnano.8b02346
Pilkington, Emily H. ; Gustafsson, Ove J.R. ; Xing, Yanting ; Hernandez-Fernaud, Juan ; Zampronio, Cleidi ; Kakinen, Aleksandr ; Faridi, Ava ; Ding, Feng ; Wilson, Paul ; Ke, Pu Chun ; Davis, Thomas P. / Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide. In: ACS Nano. 2018 ; Vol. 12, No. 6. pp. 6066-6078.
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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 corona was obtained. No trends were identified for amyloid corona proteins based on their physicochemical properties, whereas strong binding with IAPP fibrils occurred for linear proteins or multidomain proteins with structural plasticity. Proteomic analysis identified amyloid-enriched proteins that are known to play significant roles in mediating cellular machinery and processing, potentially leading to pathological outcomes and therapeutic targets.",
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Pilkington, EH, Gustafsson, OJR, Xing, Y, Hernandez-Fernaud, J, Zampronio, C, Kakinen, A, Faridi, A, Ding, F, Wilson, P, Ke, PC & Davis, TP 2018, 'Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide' ACS Nano, vol. 12, no. 6, pp. 6066-6078. https://doi.org/10.1021/acsnano.8b02346

Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide. / Pilkington, Emily H.; Gustafsson, Ove J.R.; Xing, Yanting; Hernandez-Fernaud, Juan; Zampronio, Cleidi; Kakinen, Aleksandr; Faridi, Ava; Ding, Feng; Wilson, Paul; Ke, Pu Chun; Davis, Thomas P.

In: ACS Nano, Vol. 12, No. 6, 26.06.2018, p. 6066-6078.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Gustafsson, Ove J.R.

AU - Xing, Yanting

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AU - Zampronio, Cleidi

AU - Kakinen, Aleksandr

AU - Faridi, Ava

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AU - Wilson, Paul

AU - Ke, Pu Chun

AU - Davis, Thomas P.

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AB - 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 corona was obtained. No trends were identified for amyloid corona proteins based on their physicochemical properties, whereas strong binding with IAPP fibrils occurred for linear proteins or multidomain proteins with structural plasticity. Proteomic analysis identified amyloid-enriched proteins that are known to play significant roles in mediating cellular machinery and processing, potentially leading to pathological outcomes and therapeutic targets.

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Pilkington EH, Gustafsson OJR, Xing Y, Hernandez-Fernaud J, Zampronio C, Kakinen A et al. Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide. ACS Nano. 2018 Jun 26;12(6):6066-6078. https://doi.org/10.1021/acsnano.8b02346