Pyroglutamate-modified amyloid β(3–42) monomer has more β-sheet content than the amyloid β(1

Pyroglutamate-modified amyloid β(3–42) monomer has more β-sheet content than the amyloid β(1–42) monomer

Published:2023 Issue:24 Volume:25 Page:16483-16491
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Nath Soumav¹²^ORCID,Buell Alexander K.³^ORCID,Barz Bogdan¹²^ORCID

Affiliation:

1. Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany

2. Institute of Biological Information Processing – Structural Biochemistry (IBI-7), Research Centre Jülich, Jülich, Germany

3. Department of Biotechnology and Biomedicine, Technical University of Denmark, Lyngby, Denmark

Abstract

Molecular dynamics simulations reveal key differences between Aβ(1–42) and pE-Aβ(3–42) monomers. Among these are the higher β-sheet propensity for C-terminal residues as well as increased solvent exposure of hydrophobic amino acids of pE-Aβ(3–42).

Funder

Deutsche Forschungsgemeinschaft

Novo Nordisk Fonden

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CP/D2CP05961D

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