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Daniel Otzen

Branching in amyloid fibril growth

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Branching in amyloid fibril growth. / Beyschau Andersen, Christian; Yagi, H.; Manno, M.; Martorana, V.; Ban, T.; Christiansen, Gunna; Otzen, Daniel; Goto, Yuji; Rischel, Christian.

In: Biophysical Journal, Vol. 96, No. 4, 2009, p. 1529-36.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Beyschau Andersen, C, Yagi, H, Manno, M, Martorana, V, Ban, T, Christiansen, G, Otzen, D, Goto, Y & Rischel, C 2009, 'Branching in amyloid fibril growth', Biophysical Journal, vol. 96, no. 4, pp. 1529-36. https://doi.org/10.1016/j.bpj.2008.11.024

APA

Beyschau Andersen, C., Yagi, H., Manno, M., Martorana, V., Ban, T., Christiansen, G., Otzen, D., Goto, Y., & Rischel, C. (2009). Branching in amyloid fibril growth. Biophysical Journal, 96(4), 1529-36. https://doi.org/10.1016/j.bpj.2008.11.024

CBE

Beyschau Andersen C, Yagi H, Manno M, Martorana V, Ban T, Christiansen G, Otzen D, Goto Y, Rischel C. 2009. Branching in amyloid fibril growth. Biophysical Journal. 96(4):1529-36. https://doi.org/10.1016/j.bpj.2008.11.024

MLA

Beyschau Andersen, Christian et al. "Branching in amyloid fibril growth". Biophysical Journal. 2009, 96(4). 1529-36. https://doi.org/10.1016/j.bpj.2008.11.024

Vancouver

Beyschau Andersen C, Yagi H, Manno M, Martorana V, Ban T, Christiansen G et al. Branching in amyloid fibril growth. Biophysical Journal. 2009;96(4):1529-36. https://doi.org/10.1016/j.bpj.2008.11.024

Author

Beyschau Andersen, Christian ; Yagi, H. ; Manno, M. ; Martorana, V. ; Ban, T. ; Christiansen, Gunna ; Otzen, Daniel ; Goto, Yuji ; Rischel, Christian. / Branching in amyloid fibril growth. In: Biophysical Journal. 2009 ; Vol. 96, No. 4. pp. 1529-36.

Bibtex

@article{b6096d20119311dfb95d000ea68e967b,
title = "Branching in amyloid fibril growth",
abstract = "Using the peptide hormone glucagon and Abeta(1-40) as model systems, we have sought to elucidate the mechanisms by which fibrils grow and multiply. We here present real-time observations of growing fibrils at a single-fibril level. Growing from preformed seeds, glucagon fibrils were able to generate new fibril ends by continuously branching into new fibrils. To our knowledge, this is the first time amyloid fibril branching has been observed in real-time. Glucagon fibrils formed by branching always grew in the forward direction of the parent fibril with a preferred angle of 35-40 degrees . Furthermore, branching never occurred at the tip of the parent fibril. In contrast, in a previous study by some of us, Abeta(1-40) fibrils grew exclusively by elongation of preformed seeds. Fibrillation kinetics in bulk solution were characterized by light scattering. A growth process with branching, or other processes that generate new ends from existing fibrils, should theoretically give rise to different fibrillation kinetics than growth without such a process. We show that the effect of adding seeds should be particularly different in the two cases. Our light-scattering data on glucagon and Abeta(1-40) confirm this theoretical prediction, demonstrating the central role of fibril-dependent nucleation in amyloid fibril growth.",
keywords = "Amyloid beta-Protein, Glucagon, Kinetics, Light, Microscopy, Electron, Transmission, Microscopy, Fluorescence, Peptide Fragments, Scattering, Radiation, Scattering, Small Angle, Video Recording",
author = "{Beyschau Andersen}, Christian and H. Yagi and M. Manno and V. Martorana and T. Ban and Gunna Christiansen and Daniel Otzen and Yuji Goto and Christian Rischel",
year = "2009",
doi = "10.1016/j.bpj.2008.11.024",
language = "English",
volume = "96",
pages = "1529--36",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Cell Press",
number = "4",

}

RIS

TY - JOUR

T1 - Branching in amyloid fibril growth

AU - Beyschau Andersen, Christian

AU - Yagi, H.

AU - Manno, M.

AU - Martorana, V.

AU - Ban, T.

AU - Christiansen, Gunna

AU - Otzen, Daniel

AU - Goto, Yuji

AU - Rischel, Christian

PY - 2009

Y1 - 2009

N2 - Using the peptide hormone glucagon and Abeta(1-40) as model systems, we have sought to elucidate the mechanisms by which fibrils grow and multiply. We here present real-time observations of growing fibrils at a single-fibril level. Growing from preformed seeds, glucagon fibrils were able to generate new fibril ends by continuously branching into new fibrils. To our knowledge, this is the first time amyloid fibril branching has been observed in real-time. Glucagon fibrils formed by branching always grew in the forward direction of the parent fibril with a preferred angle of 35-40 degrees . Furthermore, branching never occurred at the tip of the parent fibril. In contrast, in a previous study by some of us, Abeta(1-40) fibrils grew exclusively by elongation of preformed seeds. Fibrillation kinetics in bulk solution were characterized by light scattering. A growth process with branching, or other processes that generate new ends from existing fibrils, should theoretically give rise to different fibrillation kinetics than growth without such a process. We show that the effect of adding seeds should be particularly different in the two cases. Our light-scattering data on glucagon and Abeta(1-40) confirm this theoretical prediction, demonstrating the central role of fibril-dependent nucleation in amyloid fibril growth.

AB - Using the peptide hormone glucagon and Abeta(1-40) as model systems, we have sought to elucidate the mechanisms by which fibrils grow and multiply. We here present real-time observations of growing fibrils at a single-fibril level. Growing from preformed seeds, glucagon fibrils were able to generate new fibril ends by continuously branching into new fibrils. To our knowledge, this is the first time amyloid fibril branching has been observed in real-time. Glucagon fibrils formed by branching always grew in the forward direction of the parent fibril with a preferred angle of 35-40 degrees . Furthermore, branching never occurred at the tip of the parent fibril. In contrast, in a previous study by some of us, Abeta(1-40) fibrils grew exclusively by elongation of preformed seeds. Fibrillation kinetics in bulk solution were characterized by light scattering. A growth process with branching, or other processes that generate new ends from existing fibrils, should theoretically give rise to different fibrillation kinetics than growth without such a process. We show that the effect of adding seeds should be particularly different in the two cases. Our light-scattering data on glucagon and Abeta(1-40) confirm this theoretical prediction, demonstrating the central role of fibril-dependent nucleation in amyloid fibril growth.

KW - Amyloid beta-Protein

KW - Glucagon

KW - Kinetics

KW - Light

KW - Microscopy, Electron, Transmission

KW - Microscopy, Fluorescence

KW - Peptide Fragments

KW - Scattering, Radiation

KW - Scattering, Small Angle

KW - Video Recording

U2 - 10.1016/j.bpj.2008.11.024

DO - 10.1016/j.bpj.2008.11.024

M3 - Journal article

C2 - 19217869

VL - 96

SP - 1529

EP - 1536

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 4

ER -