Amorphous Aggregation of Amyloid Beta 1-40 Peptide in Confined Space

Chemphyschem. 2015 Nov 16;16(16):3379-84. doi: 10.1002/cphc.201500602. Epub 2015 Sep 14.

Abstract

The amorphous aggregation of Aβ1-40 peptide is addressed by using micromolding in capillaries. Both the morphology and the size of the aggregates are modulated by changing the contact angle of the sub-micrometric channel walls. Upon decreasing the hydrophilicity of the channels, the aggregates change their morphology from small aligned drops to discontinuous lines, thereby keeping their amorphous structure. Aβ1-40 fibrils are observed at high contact angles.

Keywords: Alzheimer's disease; amyloid; biotechnology; nanotechnology; scanning probe microscopy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alzheimer Disease / metabolism
  • Alzheimer Disease / pathology
  • Amyloid beta-Peptides / chemistry*
  • Amyloid beta-Peptides / metabolism
  • Biomarkers / cerebrospinal fluid
  • Dimethylpolysiloxanes / chemistry
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Microscopy, Scanning Probe
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism

Substances

  • Amyloid beta-Peptides
  • Biomarkers
  • Dimethylpolysiloxanes
  • Peptide Fragments
  • amyloid beta-protein (1-40)
  • amyloid beta-protein (1-42)
  • baysilon