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Literature DB >> 32749391

Mixing Aβ(1-40) and Aβ(1-42) peptides generates unique amyloid fibrils.

Linda Cerofolini¹, Enrico Ravera, Sara Bologna, Thomas Wiglenda, Annett Böddrich, Bettina Purfürst, Iryna Benilova, Magdalena Korsak, Gianluca Gallo, Domenico Rizzo, Leonardo Gonnelli, Marco Fragai, Bart De Strooper, Erich E Wanker, Claudio Luchinat.

Abstract

Recent structural studies show distinct morphologies for the fibrils of Aβ(1-42) and Aβ(1-40), which are believed not to co-fibrillize. We describe here a novel, structurally-uniform 1 : 1 mixed fibrillar species, which differs from both pure fibrils. It forms preferentially even when Aβ(1-42) : Aβ(1-40) peptides are mixed in a non-stoichiometric ratio.

Entities: Chemical

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Year: 2020 PMID： 32749391 DOI： 10.1039/d0cc02463e

Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222

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Cited

7 in total

1. The N-Terminal Domain of Aβ₄₀-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis.

Authors: Eva Meirovitch; Zhichun Liang; Jack H Freed
Journal: J Phys Chem B Date: 2022-02-05 Impact factor: 2.991

Review 2. Interpretable artificial intelligence and exascale molecular dynamics simulations to reveal kinetics: Applications to Alzheimer's disease.

Authors: William Martin; Gloria Sheynkman; Felice C Lightstone; Ruth Nussinov; Feixiong Cheng
Journal: Curr Opin Struct Biol Date: 2021-10-07 Impact factor: 6.809

3. Insights into Cerebral Amyloid Angiopathy Type 1 and Type 2 from Comparisons of the Fibrillar Assembly and Stability of the Aβ40-Iowa and Aβ40-Dutch Peptides.

Authors: Jitika Rajpoot; Elliot J Crooks; Brandon A Irizarry; Ashley Amundson; William E Van Nostrand; Steven O Smith
Journal: Biochemistry Date: 2022-06-06 Impact factor: 3.321

4. A lowly populated, transient β-sheet structure in monomeric Aβ^1-42 identified by multinuclear NMR of chemical denaturation.

Authors: Tayeb Kakeshpour; Venkat Ramanujam; C Ashley Barnes; Yang Shen; Jinfa Ying; Ad Bax
Journal: Biophys Chem Date: 2020-12-24 Impact factor: 2.352

Mixing Aβ(1-40) and Aβ(1-42) peptides generates unique amyloid fibrils.

1. The N-Terminal Domain of Aβ₄₀-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis.

Review 2. Interpretable artificial intelligence and exascale molecular dynamics simulations to reveal kinetics: Applications to Alzheimer's disease.

3. Insights into Cerebral Amyloid Angiopathy Type 1 and Type 2 from Comparisons of the Fibrillar Assembly and Stability of the Aβ40-Iowa and Aβ40-Dutch Peptides.

4. A lowly populated, transient β-sheet structure in monomeric Aβ^1-42 identified by multinuclear NMR of chemical denaturation.

5. Alzheimer's Aβ42 and Aβ40 form mixed oligomers with direct molecular interactions.

6. Characterizing Heparin Tetrasaccharides Binding to Amyloid-Beta Peptide.

Review 7. Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition.

Mixing Aβ(1-40) and Aβ(1-42) peptides generates unique amyloid fibrils.

1. The N-Terminal Domain of Aβ40-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis.

Review 2. Interpretable artificial intelligence and exascale molecular dynamics simulations to reveal kinetics: Applications to Alzheimer's disease.

3. Insights into Cerebral Amyloid Angiopathy Type 1 and Type 2 from Comparisons of the Fibrillar Assembly and Stability of the Aβ40-Iowa and Aβ40-Dutch Peptides.

4. A lowly populated, transient β-sheet structure in monomeric Aβ1-42 identified by multinuclear NMR of chemical denaturation.

5. Alzheimer's Aβ42 and Aβ40 form mixed oligomers with direct molecular interactions.

6. Characterizing Heparin Tetrasaccharides Binding to Amyloid-Beta Peptide.

Review 7. Amyloid Cross-Seeding: Mechanism, Implication, and Inhibition.

1. The N-Terminal Domain of Aβ₄₀-Amyloid Fibril: The MOMD Perspective of its Dynamic Structure from NMR Lineshape Analysis.

4. A lowly populated, transient β-sheet structure in monomeric Aβ^1-42 identified by multinuclear NMR of chemical denaturation.