Stop-and-go kinetics in amyloid fibrillation

Jesper Ferkinghoff-Borg; Jesper Fonslet; Christian Beyschau Andersen; Sandeep Krishna; Simone Pigolotti; Hisashi Yagi; Yuji Goto; Daniel Otzen; Mogens H Jensen

Stop-and-go kinetics in amyloid fibrillation

Jesper Ferkinghoff-Borg, Jesper Fonslet, Christian Beyschau Andersen, Sandeep Krishna, Simone Pigolotti, Hisashi Yagi, Yuji Goto, Daniel Otzen, Mogens H Jensen

Department of Chemistry - Center for Uopløselige Proteinstrukturer

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

43 Citations (Scopus)

Abstract

Many human diseases are associated with protein aggregation and fibrillation. We present experiments on in vitro glucagon fibrillation using total internal reflection fluorescence microscopy, providing real-time measurements of single-fibril growth. We find that amyloid fibrils grow in an intermittent fashion, with periods of growth followed by long pauses. The observed exponential distributions of stop and growth times support a Markovian model, in which fibrils shift between the two states with specific rates. Even if the individual rates vary considerably, we observe that the probability of being in the growing (stopping) state is very close to 1/4 (3/4) in all experiments.

Original language	English
Journal	Physical Review E. Statistical, Nonlinear, and Soft Matter Physics
Volume	82
Issue	1 Pt 1
Pages (from-to)	010901
ISSN	1063-651X
Publication status	Published - 1 Jul 2010

Keywords

Amyloid
Computer Simulation
Crystallization
Kinetics
Models, Chemical
Models, Molecular
Multiprotein Complexes
Protein Conformation

Cite this

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title = "Stop-and-go kinetics in amyloid fibrillation",

abstract = "Many human diseases are associated with protein aggregation and fibrillation. We present experiments on in vitro glucagon fibrillation using total internal reflection fluorescence microscopy, providing real-time measurements of single-fibril growth. We find that amyloid fibrils grow in an intermittent fashion, with periods of growth followed by long pauses. The observed exponential distributions of stop and growth times support a Markovian model, in which fibrils shift between the two states with specific rates. Even if the individual rates vary considerably, we observe that the probability of being in the growing (stopping) state is very close to 1/4 (3/4) in all experiments.",

keywords = "Amyloid, Computer Simulation, Crystallization, Kinetics, Models, Chemical, Models, Molecular, Multiprotein Complexes, Protein Conformation",

author = "Jesper Ferkinghoff-Borg and Jesper Fonslet and Andersen, {Christian Beyschau} and Sandeep Krishna and Simone Pigolotti and Hisashi Yagi and Yuji Goto and Daniel Otzen and Jensen, {Mogens H}",

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Stop-and-go kinetics in amyloid fibrillation. / Ferkinghoff-Borg, Jesper; Fonslet, Jesper; Andersen, Christian Beyschau et al.
In: Physical Review E. Statistical, Nonlinear, and Soft Matter Physics, Vol. 82, No. 1 Pt 1, 01.07.2010, p. 010901.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Stop-and-go kinetics in amyloid fibrillation

AU - Ferkinghoff-Borg, Jesper

AU - Fonslet, Jesper

AU - Andersen, Christian Beyschau

AU - Krishna, Sandeep

AU - Pigolotti, Simone

AU - Yagi, Hisashi

AU - Goto, Yuji

AU - Otzen, Daniel

AU - Jensen, Mogens H

PY - 2010/7/1

Y1 - 2010/7/1

N2 - Many human diseases are associated with protein aggregation and fibrillation. We present experiments on in vitro glucagon fibrillation using total internal reflection fluorescence microscopy, providing real-time measurements of single-fibril growth. We find that amyloid fibrils grow in an intermittent fashion, with periods of growth followed by long pauses. The observed exponential distributions of stop and growth times support a Markovian model, in which fibrils shift between the two states with specific rates. Even if the individual rates vary considerably, we observe that the probability of being in the growing (stopping) state is very close to 1/4 (3/4) in all experiments.

AB - Many human diseases are associated with protein aggregation and fibrillation. We present experiments on in vitro glucagon fibrillation using total internal reflection fluorescence microscopy, providing real-time measurements of single-fibril growth. We find that amyloid fibrils grow in an intermittent fashion, with periods of growth followed by long pauses. The observed exponential distributions of stop and growth times support a Markovian model, in which fibrils shift between the two states with specific rates. Even if the individual rates vary considerably, we observe that the probability of being in the growing (stopping) state is very close to 1/4 (3/4) in all experiments.

KW - Amyloid

KW - Computer Simulation

KW - Crystallization

KW - Kinetics

KW - Models, Chemical

KW - Models, Molecular

KW - Multiprotein Complexes

KW - Protein Conformation

M3 - Journal article

C2 - 20866557

SN - 1063-651X

VL - 82

SP - 010901

JO - Physical Review E. Statistical, Nonlinear, and Soft Matter Physics

JF - Physical Review E. Statistical, Nonlinear, and Soft Matter Physics

IS - 1 Pt 1

ER -

Stop-and-go kinetics in amyloid fibrillation

Abstract

Keywords

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