European Biophysics Journal

, Volume 38, Issue 8, pp 1135–1140

Dehydration stability of amyloid fibrils studied by AFM

  • Gjertrud Maurstad
  • Marcus Prass
  • Louise C. Serpell
  • Pawel Sikorski
Original Paper

DOI: 10.1007/s00249-009-0526-x

Cite this article as:
Maurstad, G., Prass, M., Serpell, L.C. et al. Eur Biophys J (2009) 38: 1135. doi:10.1007/s00249-009-0526-x
  • 282 Downloads

Abstract

Atomic force microscopy was used to investigate the stability of dehydrated amyloid fibrils formed by human islet polypeptide (IAPP) and Aβ(1–42) peptides. IAPP amyloid fibrils were imaged in liquid (hydrated state) and in air (dehydrated). In addition, fibrils dried on the mica surface were rehydrated and re-examined both in liquid and in air (after consecutive redrying). As reported previously, the initial drying process does not result in any major change in the amyloid appearance and the dimensions of the fibrils are preserved. However, when once-dried samples are rehydrated, fibril stability is lost. The fibrils disintegrate into small particles that are attached to the mica surface. This process is further confirmed by studies of the rehydrated samples after drying, on which the morphology of the fibrils is clearly changed. Similar behavior is observed for Aβ(1–42) amyloid fibrils, which are apparently stable on first drying, but disintegrate on rehydration. The observed change indicates that dehydration is causing a change in the internal structure of the amyloid fibrils. This has important implications for studies of amyloid fibrils by other techniques. Due to the potential influence of hydration and sample history on amyloid structure, preparation and study of amyloid samples with controlled humidity requires more consideration.

Keywords

AFM Peptide Protein Aggregation Amyloid 

Copyright information

© European Biophysical Societies' Association 2009

Authors and Affiliations

  • Gjertrud Maurstad
    • 1
  • Marcus Prass
    • 1
    • 3
  • Louise C. Serpell
    • 2
  • Pawel Sikorski
    • 1
  1. 1.Department of PhysicsNorwegian University of Science and TechnologyTrondheimNorway
  2. 2.Department of Chemistry and Biochemistry, School of Life SciencesUniversity of SussexFalmerUK
  3. 3.Institute of BiophysicsUniversity of BremenBremenGermany

Personalised recommendations