Reversible mechanical unzipping of amyloid β-fibrils

M. Kellermayer, L. Grama, Árpád Karsai, A. Nagy, Amram Kahn, Zsolt L. Datki, B. Penke

Research output: Contribution to journalArticle

69 Citations (Scopus)

Abstract

Amyloid fibrils are self-associating filamentous structures, the deposition of which is considered to be one of the most important factors in the pathogenesis of Alzheimer's disease and various other disorders. Here we used single molecule manipulation methods to explore the mechanics and structural dynamics of amyloid fibrils. In mechanically manipulated amyloid fibrils, formed from either amyloid β (Aβ) peptides 1-40 or 25-35, β-sheets behave as elastic structures that can be "unzipped" from the fibril with constant forces. The unzipping forces were different for Aβ1-40 and Aβ25-35. Unzipping was fully reversible across a wide range of stretch rates provided that coupling, via the β-sheet, between bound and dissociated states was maintained. The rapid, cooperative zipping together of β-sheets could be an important mechanism behind the self-assembly of amyloid fibrils. The repetitive force patterns contribute to a mechanical fingerprint that could be utilized in the characterization of different amyloid fibrils.

Original languageEnglish
Pages (from-to)8464-8470
Number of pages7
JournalJournal of Biological Chemistry
Volume280
Issue number9
DOIs
Publication statusPublished - Mar 4 2005

Fingerprint

Amyloid
Structural dynamics
Dermatoglyphics
Mechanics
Self assembly
Alzheimer Disease
Peptides
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

Reversible mechanical unzipping of amyloid β-fibrils. / Kellermayer, M.; Grama, L.; Karsai, Árpád; Nagy, A.; Kahn, Amram; Datki, Zsolt L.; Penke, B.

In: Journal of Biological Chemistry, Vol. 280, No. 9, 04.03.2005, p. 8464-8470.

Research output: Contribution to journalArticle

Kellermayer, M. ; Grama, L. ; Karsai, Árpád ; Nagy, A. ; Kahn, Amram ; Datki, Zsolt L. ; Penke, B. / Reversible mechanical unzipping of amyloid β-fibrils. In: Journal of Biological Chemistry. 2005 ; Vol. 280, No. 9. pp. 8464-8470.
@article{757b0f56d4444203adfd3d8cb944ff20,
title = "Reversible mechanical unzipping of amyloid β-fibrils",
abstract = "Amyloid fibrils are self-associating filamentous structures, the deposition of which is considered to be one of the most important factors in the pathogenesis of Alzheimer's disease and various other disorders. Here we used single molecule manipulation methods to explore the mechanics and structural dynamics of amyloid fibrils. In mechanically manipulated amyloid fibrils, formed from either amyloid β (Aβ) peptides 1-40 or 25-35, β-sheets behave as elastic structures that can be {"}unzipped{"} from the fibril with constant forces. The unzipping forces were different for Aβ1-40 and Aβ25-35. Unzipping was fully reversible across a wide range of stretch rates provided that coupling, via the β-sheet, between bound and dissociated states was maintained. The rapid, cooperative zipping together of β-sheets could be an important mechanism behind the self-assembly of amyloid fibrils. The repetitive force patterns contribute to a mechanical fingerprint that could be utilized in the characterization of different amyloid fibrils.",
author = "M. Kellermayer and L. Grama and {\'A}rp{\'a}d Karsai and A. Nagy and Amram Kahn and Datki, {Zsolt L.} and B. Penke",
year = "2005",
month = "3",
day = "4",
doi = "10.1074/jbc.M411556200",
language = "English",
volume = "280",
pages = "8464--8470",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "9",

}

TY - JOUR

T1 - Reversible mechanical unzipping of amyloid β-fibrils

AU - Kellermayer, M.

AU - Grama, L.

AU - Karsai, Árpád

AU - Nagy, A.

AU - Kahn, Amram

AU - Datki, Zsolt L.

AU - Penke, B.

PY - 2005/3/4

Y1 - 2005/3/4

N2 - Amyloid fibrils are self-associating filamentous structures, the deposition of which is considered to be one of the most important factors in the pathogenesis of Alzheimer's disease and various other disorders. Here we used single molecule manipulation methods to explore the mechanics and structural dynamics of amyloid fibrils. In mechanically manipulated amyloid fibrils, formed from either amyloid β (Aβ) peptides 1-40 or 25-35, β-sheets behave as elastic structures that can be "unzipped" from the fibril with constant forces. The unzipping forces were different for Aβ1-40 and Aβ25-35. Unzipping was fully reversible across a wide range of stretch rates provided that coupling, via the β-sheet, between bound and dissociated states was maintained. The rapid, cooperative zipping together of β-sheets could be an important mechanism behind the self-assembly of amyloid fibrils. The repetitive force patterns contribute to a mechanical fingerprint that could be utilized in the characterization of different amyloid fibrils.

AB - Amyloid fibrils are self-associating filamentous structures, the deposition of which is considered to be one of the most important factors in the pathogenesis of Alzheimer's disease and various other disorders. Here we used single molecule manipulation methods to explore the mechanics and structural dynamics of amyloid fibrils. In mechanically manipulated amyloid fibrils, formed from either amyloid β (Aβ) peptides 1-40 or 25-35, β-sheets behave as elastic structures that can be "unzipped" from the fibril with constant forces. The unzipping forces were different for Aβ1-40 and Aβ25-35. Unzipping was fully reversible across a wide range of stretch rates provided that coupling, via the β-sheet, between bound and dissociated states was maintained. The rapid, cooperative zipping together of β-sheets could be an important mechanism behind the self-assembly of amyloid fibrils. The repetitive force patterns contribute to a mechanical fingerprint that could be utilized in the characterization of different amyloid fibrils.

UR - http://www.scopus.com/inward/record.url?scp=14844327767&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=14844327767&partnerID=8YFLogxK

U2 - 10.1074/jbc.M411556200

DO - 10.1074/jbc.M411556200

M3 - Article

C2 - 15596431

AN - SCOPUS:14844327767

VL - 280

SP - 8464

EP - 8470

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 9

ER -