Compact fibril-like structure of amyloid β-peptide (1–42) monomers-Reference-Cited by-同舟云学术

Compact fibril-like structure of amyloid β-peptide (1–42) monomers

Published:2021 Issue:7 Volume:57 Page:947-950
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Barz Bogdan¹²³⁴⁵^ORCID,Buell Alexander K.⁶⁷⁸⁹^ORCID,Nath Soumav¹²³⁴⁵^ORCID

Affiliation:

1. Institut für Physikalische Biologie

2. Heinrich-Heine-Universität Düsseldorf

3. Düsseldorf

4. Germany

5. Institute of Biological Information Processing – Structural Biochemistry (IBI-7)

6. Department of Biotechnology and Biomedicine

7. Technical University of Denmark

8. Lyngby

9. Denmark

Abstract

Amyloid β (Aβ) monomers sample a random-coil type of conformation in water with a tendency to adopt compact structures with fibril-like features.

Funder

Deutsche Forschungsgemeinschaft

Novo Nordisk Fonden

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2021/CC/D0CC06607A

Reference36 articles.

1. The amyloid state and its association with protein misfolding diseases

2. A partially folded structure of amyloid-beta(1–40) in an aqueous environment

3. Monomeric Aβ1–40 and Aβ1–42 Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil

4. Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies

5. High-resolution probing of early events in amyloid-β aggregation related to Alzheimer's disease

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