Amyloid β-peptides 1–40 and 1–42 form oligomers with mixed β-sheets
Author:
Affiliation:
1. Department of Biochemistry and Biophysics
2. Stockholm University
3. Arrhenius Laboratories
4. 10691 Stockholm
5. Sweden
6. Department of Medical Biochemistry and Biophysics
7. Umeå University
8. 90187 Umeå
Abstract
Aβ40 and Aβ42 co-aggregate and form oligomers with mixed β-sheets as revealed by isotope-edited infrared spectroscopy.
Funder
Stiftelsen Lars Hiertas Minne
Alzheimerfonden
Knut och Alice Wallenbergs Stiftelse
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2017/SC/C7SC01743J
Reference52 articles.
1. Peptide Compositions of the Cerebrovascular and Senile Plaque Core Amyloid Deposits of Alzheimer′s Disease
2. Familial Alzheimer's Disease–Linked Presenilin 1 Variants Elevate Aβ1–42/1–40 Ratio In Vitro and In Vivo
3. Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
4. An Increased Percentage of Long Amyloid β Protein Secreted by Familial Amyloid β Protein Precursor (βApp 717 ) Mutants
5. Mean age-of-onset of familial alzheimer disease caused by presenilin mutations correlates with both increased Aβ42 and decreased Aβ40
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