Thermally-induced effects in oriented network of amyloid β25-35 fibrils

M. Kolsofszki, Á Karsai, K. Soós, B. Penke, M. Kellermayer

Research output: Chapter in Book/Report/Conference proceedingConference contribution

2 Citations (Scopus)

Abstract

Amyloid fibrils are filamentous protein deposits in the extracellular space of various tissues in neurodegenerative and protein misfolding diseases. They may be used in nanotechnology applications because of their self-assembly properties and stability. Recently we have shown that amyloid beta 25-35 (Aβ25-35) forms a highly oriented, K+-dependent network on mica, and its mutant form (Aβ25-35-N27C) may be chemically addressed for functionalization in dedicated applications. In the present work we investigated thermally-induced changes in the morphology of the oriented Aβ25-35 fibril network. The fibrils maintained a high orientation stability in the temperature range of 30-70°C, suggesting that orientational rearrangement of Aβ25-35 fibrils on mica is an unfavorable process. Above ∼45°C a gradual decrease in fibril length and dissociation from the surface could be observed. Furthermore, at high temperatures (45-70°C) the average fibril thickness increased, indicating changes in the underlying structure or structural dynamics. Possibly, a thermally induced transition in the Aβ25-35 peptide around 45°C leads to structural changes in the fibril as well. The temperature-dependent changes need to be considered in the use of amyloid fibrils in nanotechnology applications.

Original languageEnglish
Title of host publicationProgress in Colloid and Polymer Science
Pages169-173
Number of pages5
Volume135
DOIs
Publication statusPublished - 2008

Publication series

NameProgress in Colloid and Polymer Science
Volume135
ISSN (Print)0340255X

Fingerprint

Amyloid
nanotechnology
mica
proteins
Nanotechnology
dynamic structural analysis
Mica
peptides
self assembly
deposits
dissociation
Structural dynamics
temperature
Proteins
Temperature
Self assembly
Deposits
amyloid beta-protein (25-35)
Tissue
Peptides

Keywords

  • Amyloid fibril
  • Atomic force microscopy
  • Heat stability
  • Intrafibrillar interactions
  • Structural transition

ASJC Scopus subject areas

  • Organic Chemistry
  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry
  • Materials Chemistry
  • Polymers and Plastics

Cite this

Kolsofszki, M., Karsai, Á., Soós, K., Penke, B., & Kellermayer, M. (2008). Thermally-induced effects in oriented network of amyloid β25-35 fibrils. In Progress in Colloid and Polymer Science (Vol. 135, pp. 169-173). (Progress in Colloid and Polymer Science; Vol. 135). https://doi.org/10.1007/2882-2008-109

Thermally-induced effects in oriented network of amyloid β25-35 fibrils. / Kolsofszki, M.; Karsai, Á; Soós, K.; Penke, B.; Kellermayer, M.

Progress in Colloid and Polymer Science. Vol. 135 2008. p. 169-173 (Progress in Colloid and Polymer Science; Vol. 135).

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Kolsofszki, M, Karsai, Á, Soós, K, Penke, B & Kellermayer, M 2008, Thermally-induced effects in oriented network of amyloid β25-35 fibrils. in Progress in Colloid and Polymer Science. vol. 135, Progress in Colloid and Polymer Science, vol. 135, pp. 169-173. https://doi.org/10.1007/2882-2008-109
Kolsofszki M, Karsai Á, Soós K, Penke B, Kellermayer M. Thermally-induced effects in oriented network of amyloid β25-35 fibrils. In Progress in Colloid and Polymer Science. Vol. 135. 2008. p. 169-173. (Progress in Colloid and Polymer Science). https://doi.org/10.1007/2882-2008-109
Kolsofszki, M. ; Karsai, Á ; Soós, K. ; Penke, B. ; Kellermayer, M. / Thermally-induced effects in oriented network of amyloid β25-35 fibrils. Progress in Colloid and Polymer Science. Vol. 135 2008. pp. 169-173 (Progress in Colloid and Polymer Science).
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