Probing the secondary structure of individual Aβ40 amorphous aggregates and fibrils by AFM-IR spectroscopy

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Probing the secondary structure of individual Aβ40 amorphous aggregates and fibrils by AFM-IR spectroscopy. / Herzberg, Mikkel; Szunyogh, Daniel; Thulstrup, Peter W; Hassenkam, Tue; Hemmingsen, Lars.

In: ChemBioChem, 2020, p. 3521-3524.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Herzberg, M, Szunyogh, D, Thulstrup, PW, Hassenkam, T & Hemmingsen, L 2020, 'Probing the secondary structure of individual Aβ40 amorphous aggregates and fibrils by AFM-IR spectroscopy', ChemBioChem, pp. 3521-3524. https://doi.org/10.1002/cbic.202000632

APA

Herzberg, M., Szunyogh, D., Thulstrup, P. W., Hassenkam, T., & Hemmingsen, L. (2020). Probing the secondary structure of individual Aβ40 amorphous aggregates and fibrils by AFM-IR spectroscopy. ChemBioChem, 3521-3524. https://doi.org/10.1002/cbic.202000632

Vancouver

Herzberg M, Szunyogh D, Thulstrup PW, Hassenkam T, Hemmingsen L. Probing the secondary structure of individual Aβ40 amorphous aggregates and fibrils by AFM-IR spectroscopy. ChemBioChem. 2020;3521-3524. https://doi.org/10.1002/cbic.202000632

Author

Herzberg, Mikkel ; Szunyogh, Daniel ; Thulstrup, Peter W ; Hassenkam, Tue ; Hemmingsen, Lars. / Probing the secondary structure of individual Aβ40 amorphous aggregates and fibrils by AFM-IR spectroscopy. In: ChemBioChem. 2020 ; pp. 3521-3524.

Bibtex

@article{e4aabd2f373945ab8d5c16274c2e991e,
title = "Probing the secondary structure of individual Aβ40 amorphous aggregates and fibrils by AFM-IR spectroscopy",
abstract = "Structural characterization of aggregates and fibrils of the Aβ protein is pivotal to the molecular level elucidation of Alzheimer's disease (AD). AFM-IR provides nanoscale resolution, and thus allows for spectroscopic interrogation of individual aggregates and fibrils. During aggregation of Aβ we observed mainly disordered Aβ at t=15 min, substantial structural diversity including co-existence of parallel and antiparallel β-sheets within a large amorphous aggregate at t=2 hours, while fibrils exhibited the expected signature of parallel β-sheets at t=1 week. The resonance observed for parallel β-sheets at t=2 hours coincides with that observed for fibrils (at 1634 cm-1), indicating that fibril-like species exist within the large aggregates. Thus, nucleation might occur within such species, in analogy to current theories of protein crystallization where nucleation occurs within large protein clusters. Cu2+ perturbs Aβ aggregation, catalysing rapid formation of amorphous aggregates with diverse secondary structure, but inhibiting fibril growth.",
author = "Mikkel Herzberg and Daniel Szunyogh and Thulstrup, {Peter W} and Tue Hassenkam and Lars Hemmingsen",
note = "{\textcopyright} 2020 Wiley-VCH GmbH.",
year = "2020",
doi = "10.1002/cbic.202000632",
language = "English",
pages = "3521--3524",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley - V C H Verlag GmbH & Co. KGaA",

}

RIS

TY - JOUR

T1 - Probing the secondary structure of individual Aβ40 amorphous aggregates and fibrils by AFM-IR spectroscopy

AU - Herzberg, Mikkel

AU - Szunyogh, Daniel

AU - Thulstrup, Peter W

AU - Hassenkam, Tue

AU - Hemmingsen, Lars

N1 - © 2020 Wiley-VCH GmbH.

PY - 2020

Y1 - 2020

N2 - Structural characterization of aggregates and fibrils of the Aβ protein is pivotal to the molecular level elucidation of Alzheimer's disease (AD). AFM-IR provides nanoscale resolution, and thus allows for spectroscopic interrogation of individual aggregates and fibrils. During aggregation of Aβ we observed mainly disordered Aβ at t=15 min, substantial structural diversity including co-existence of parallel and antiparallel β-sheets within a large amorphous aggregate at t=2 hours, while fibrils exhibited the expected signature of parallel β-sheets at t=1 week. The resonance observed for parallel β-sheets at t=2 hours coincides with that observed for fibrils (at 1634 cm-1), indicating that fibril-like species exist within the large aggregates. Thus, nucleation might occur within such species, in analogy to current theories of protein crystallization where nucleation occurs within large protein clusters. Cu2+ perturbs Aβ aggregation, catalysing rapid formation of amorphous aggregates with diverse secondary structure, but inhibiting fibril growth.

AB - Structural characterization of aggregates and fibrils of the Aβ protein is pivotal to the molecular level elucidation of Alzheimer's disease (AD). AFM-IR provides nanoscale resolution, and thus allows for spectroscopic interrogation of individual aggregates and fibrils. During aggregation of Aβ we observed mainly disordered Aβ at t=15 min, substantial structural diversity including co-existence of parallel and antiparallel β-sheets within a large amorphous aggregate at t=2 hours, while fibrils exhibited the expected signature of parallel β-sheets at t=1 week. The resonance observed for parallel β-sheets at t=2 hours coincides with that observed for fibrils (at 1634 cm-1), indicating that fibril-like species exist within the large aggregates. Thus, nucleation might occur within such species, in analogy to current theories of protein crystallization where nucleation occurs within large protein clusters. Cu2+ perturbs Aβ aggregation, catalysing rapid formation of amorphous aggregates with diverse secondary structure, but inhibiting fibril growth.

U2 - 10.1002/cbic.202000632

DO - 10.1002/cbic.202000632

M3 - Journal article

C2 - 33027846

SP - 3521

EP - 3524

JO - ChemBioChem

JF - ChemBioChem

SN - 1439-4227

ER -

ID: 249626251