Aggregation prone amyloid-β⋅CuII Species formed on the millisecond timescale at mildly acidic conditions

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Aggregation prone amyloid-β⋅CuII Species formed on the millisecond timescale at mildly acidic conditions. / Pedersen, Jeppe Trudslev; Borg, Christian Bernsen; Michaels, Thomas C. T.; Knowles, Tuomas P. J.; Faller, Peter; Teilum, Kaare; Hemmingsen, Lars Bo Stegeager.

I: ChemBioChem, Bind 16, Nr. 9, 2015, s. 1293-1297.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Pedersen, JT, Borg, CB, Michaels, TCT, Knowles, TPJ, Faller, P, Teilum, K & Hemmingsen, LBS 2015, 'Aggregation prone amyloid-β⋅CuII Species formed on the millisecond timescale at mildly acidic conditions', ChemBioChem, bind 16, nr. 9, s. 1293-1297. https://doi.org/10.1002/cbic.201500080

APA

Pedersen, J. T., Borg, C. B., Michaels, T. C. T., Knowles, T. P. J., Faller, P., Teilum, K., & Hemmingsen, L. B. S. (2015). Aggregation prone amyloid-β⋅CuII Species formed on the millisecond timescale at mildly acidic conditions. ChemBioChem, 16(9), 1293-1297. https://doi.org/10.1002/cbic.201500080

Vancouver

Pedersen JT, Borg CB, Michaels TCT, Knowles TPJ, Faller P, Teilum K o.a. Aggregation prone amyloid-β⋅CuII Species formed on the millisecond timescale at mildly acidic conditions. ChemBioChem. 2015;16(9):1293-1297. https://doi.org/10.1002/cbic.201500080

Author

Pedersen, Jeppe Trudslev ; Borg, Christian Bernsen ; Michaels, Thomas C. T. ; Knowles, Tuomas P. J. ; Faller, Peter ; Teilum, Kaare ; Hemmingsen, Lars Bo Stegeager. / Aggregation prone amyloid-β⋅CuII Species formed on the millisecond timescale at mildly acidic conditions. I: ChemBioChem. 2015 ; Bind 16, Nr. 9. s. 1293-1297.

Bibtex

@article{e5d98a9f2d09489181a9817a35a4dadb,
title = "Aggregation prone amyloid-β⋅CuII Species formed on the millisecond timescale at mildly acidic conditions",
abstract = "Metal ions and their interaction with the amyloid beta (Aβ) peptide might be key elements in the development of Alzheimer's disease. In this work the effect of CuII on the aggregation of Aβ is explored on a timescale from milliseconds to days, both at physiological pH and under mildly acidic conditions, by using stopped-flow kinetic measurements (fluorescence and light-scattering), 1H NMR relaxation and ThT fluorescence. A minimal reaction model that relates the initial CuII binding and Aβ folding with downstream aggregation is presented. We demonstrate that a highly aggregation prone Aβ⋅CuII species is formed on the sub-second timescale at mildly acidic pH. This observation might be central to the molecular origin of the known detrimental effect of acidosis in Alzheimer's disease.",
author = "Pedersen, {Jeppe Trudslev} and Borg, {Christian Bernsen} and Michaels, {Thomas C. T.} and Knowles, {Tuomas P. J.} and Peter Faller and Kaare Teilum and Hemmingsen, {Lars Bo Stegeager}",
year = "2015",
doi = "10.1002/cbic.201500080",
language = "English",
volume = "16",
pages = "1293--1297",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",
number = "9",

}

RIS

TY - JOUR

T1 - Aggregation prone amyloid-β⋅CuII Species formed on the millisecond timescale at mildly acidic conditions

AU - Pedersen, Jeppe Trudslev

AU - Borg, Christian Bernsen

AU - Michaels, Thomas C. T.

AU - Knowles, Tuomas P. J.

AU - Faller, Peter

AU - Teilum, Kaare

AU - Hemmingsen, Lars Bo Stegeager

PY - 2015

Y1 - 2015

N2 - Metal ions and their interaction with the amyloid beta (Aβ) peptide might be key elements in the development of Alzheimer's disease. In this work the effect of CuII on the aggregation of Aβ is explored on a timescale from milliseconds to days, both at physiological pH and under mildly acidic conditions, by using stopped-flow kinetic measurements (fluorescence and light-scattering), 1H NMR relaxation and ThT fluorescence. A minimal reaction model that relates the initial CuII binding and Aβ folding with downstream aggregation is presented. We demonstrate that a highly aggregation prone Aβ⋅CuII species is formed on the sub-second timescale at mildly acidic pH. This observation might be central to the molecular origin of the known detrimental effect of acidosis in Alzheimer's disease.

AB - Metal ions and their interaction with the amyloid beta (Aβ) peptide might be key elements in the development of Alzheimer's disease. In this work the effect of CuII on the aggregation of Aβ is explored on a timescale from milliseconds to days, both at physiological pH and under mildly acidic conditions, by using stopped-flow kinetic measurements (fluorescence and light-scattering), 1H NMR relaxation and ThT fluorescence. A minimal reaction model that relates the initial CuII binding and Aβ folding with downstream aggregation is presented. We demonstrate that a highly aggregation prone Aβ⋅CuII species is formed on the sub-second timescale at mildly acidic pH. This observation might be central to the molecular origin of the known detrimental effect of acidosis in Alzheimer's disease.

U2 - 10.1002/cbic.201500080

DO - 10.1002/cbic.201500080

M3 - Journal article

C2 - 25989377

VL - 16

SP - 1293

EP - 1297

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

IS - 9

ER -

ID: 132940188