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Effect of packing density of lipid vesicles on the Aβ42 fibril polymorphism

Chae Eun Heo1, Chae Ri Park1, Hugh I Kim1

  • 1Department of Chemistry, Korea University, Seoul, 02841, Republic of Korea; Center for Proteogenome Research, Korea University, Seoul, 02841, Republic of Korea.

Chemistry and Physics of Lipids
|March 6, 2021
PubMed

Insights

Lipid packing density significantly impacts amyloid-β 1-42 (Aβ42) fibrillation, influencing Alzheimer

Area of Science:

  • Biochemistry
  • Neuroscience
  • Materials Science

Background:

  • Amyloid-β 1-42 (Aβ42) aggregation on lipid membranes is a key factor in Alzheimer's disease (AD) pathology.
  • Understanding the influence of lipid properties on Aβ42 fibrillation is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the effect of lipid vesicle packing density on Aβ42 fibrillation kinetics and morphology.
  • To elucidate the role of different lipid types, including phosphatidylcholines (PCs) and anionic lipids, in modulating Aβ42 aggregation.

Main Methods:

  • Utilized three distinct phosphatidylcholine (PC) lipids with varying numbers of cis-double bonds to control lipid packing density.
  • Investigated Aβ42 fibrillation kinetics and fibril morphology using dioleoyl phosphatidylcholine (DOPC), dioleoyl phosphatidylserine (DOPS), and dioleoyl phosphatidylglycerol (DOPG) vesicles, as well as mixed lipid compositions.
  • Analyzed the interactions between Aβ42 and lipid membranes, considering both hydrophobic and electrostatic interactions.

Main Results:

  • Increased double bonds in lipid acyl chains led to enhanced Aβ42 fibrillation and shorter fibril formation.
  • Loosely packed DOPC membranes facilitated rapid Aβ42 fibrillation and short fibril morphologies due to hydrophobic interactions.
  • Anionic lipids (DOPS, DOPG) and mixed vesicles suppressed Aβ42 fibrillation modulation compared to loosely packed membranes, attributed to electrostatic interactions.

Conclusions:

  • Lipid packing density is a critical determinant of Aβ42 fibrillation kinetics and morphology.
  • Hydrophobic interactions with loosely packed lipid acyl chains accelerate fibrillation, while electrostatic interactions with anionic lipids can suppress it.
  • This study provides a mechanistic understanding of lipid-associated amyloid fibrillations, relevant to Alzheimer's disease pathogenesis.
Keywords:
Amyloid fibrillationAmyloid-βLipid associated amyloid fibrillationPacking densityPhosphatidylcholinePolymorphism

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