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Polymorphism in disease-related apolipoprotein C-II amyloid fibrils: a structural model for rod-like fibrils

Courtney O Zlatic1,2, Yu Mao1,2, Nevena Todorova3

  • 1Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Vic., Australia.

The FEBS Journal
|May 24, 2018
PubMed

Insights

Human apolipoprotein C-II forms amyloid fibrils linked to cardiovascular disease. Lipid presence alters fibril structure, influencing disease mechanisms and potential therapeutic targets.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cardiovascular Disease Research

Background:

  • Human apolipoprotein C-II (apoC-II) self-assembles into amyloid fibrils.
  • ApoC-II amyloid deposits are associated with cardiovascular disease.
  • Lipid presence influences apoC-II fibril morphology.

Purpose of the Study:

  • To investigate the structural basis of lipid-dependent apoC-II fibril polymorphism.
  • To elucidate the structural features of rod-like apoC-II fibrils.

Main Methods:

  • Hydrogen-deuterium exchange and NMR spectroscopy for structural analysis.
  • Molecular dynamics simulations to model fibril arrangements.
  • X-ray fiber diffraction to determine fibril spacing.

Main Results:

  • Rod-like apoC-II fibrils exhibit a cross-β structure in the C-terminal region (58-76).
  • Molecular dynamics favored a parallel cross-β fibril structure.
  • X-ray fiber diffraction revealed specific spacings indicative of an antiparallel fibril arrangement.

Conclusions:

  • Lipid-dependent structural polymorphism of apoC-II fibrils influences their properties.
  • Understanding these structures is crucial for elucidating apoC-II's role in renal amyloidosis and cardiovascular disease.
Keywords:
amyloid fibrilsapolipoprotein C-IIcross-beta structurepolymorphismprotein misfolding

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