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Myelin basic protein binds to and inhibits the fibrillar assembly of Abeta42 in vitro

Michael D Hoos1, Mahiuddin Ahmed, Steven O Smith

  • 1Department of Medicine, Stony Brook University, Stony Brook, New York 11794-8153, USA.

Biochemistry
|April 24, 2009
PubMed

Insights

Myelin basic protein (MBP) inhibits amyloid beta-protein (Abeta) fibril formation. This suggests MBP may regulate Abeta42 deposition and early amyloid plaque formation in Alzheimer's disease.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Alzheimer's disease is characterized by amyloid beta-protein (Abeta) plaque deposition in the brain.
  • Abeta peptides, particularly Abeta42, are prone to forming fibrils and are implicated in early plaque formation.
  • Familial forms of cerebral amyloid angiopathy involve mutations in Abeta peptides.

Purpose of the Study:

  • To investigate the effect of myelin basic protein (MBP) on the fibrillar assembly of normal Abeta42 peptides.
  • To determine if MBP's inhibitory effects extend to non-mutated Abeta42, similar to its effect on mutated Abeta peptides.

Main Methods:

  • Biochemical assays to assess fibril formation.
  • Ultrastructural techniques to visualize fibril assembly.
  • Studies on the interaction between MBP and Abeta42 peptides.

Main Results:

  • Myelin basic protein (MBP) effectively inhibits the beta-sheet fibrillar assembly of Abeta42 peptides.
  • MBP demonstrated inhibitory effects on both mutated and normal Abeta42 peptides.
  • Biochemical and ultrastructural data confirmed MBP's anti-fibrillogenic activity against Abeta42.

Conclusions:

  • Myelin basic protein (MBP) can inhibit the formation of Abeta42 fibrils.
  • MBP may play a regulatory role in controlling Abeta42 deposition.
  • These findings suggest a potential mechanism for modulating early amyloid plaque formation in Alzheimer's disease.

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