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Literature DB >> 24471163

Early amyloid β-protein aggregation precedes conformational change.

Bogdan Barz¹, Olujide O Olubiyi, Birgit Strodel.

Abstract

The aggregation of amyloid-β protein (1-42) is studied at experimental concentrations using all-atom molecular dynamics simulations. We observe a fast aggregation into oligomers without significant changes in the internal structure of individual proteins. The aggregation process is characterized in terms of transition networks.

Mesh：

Substances：
Amyloid beta-Peptides

Year: 2014 PMID： 24471163 DOI： 10.1039/c3cc48704k

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

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Cited

12 in total

Review 1. Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.

Authors: Jessica Nasica-Labouze; Phuong H Nguyen; Fabio Sterpone; Olivia Berthoumieu; Nicolae-Viorel Buchete; Sébastien Coté; Alfonso De Simone; Andrew J Doig; Peter Faller; Angel Garcia; Alessandro Laio; Mai Suan Li; Simone Melchionna; Normand Mousseau; Yuguang Mu; Anant Paravastu; Samuela Pasquali; David J Rosenman; Birgit Strodel; Bogdan Tarus; John H Viles; Tong Zhang; Chunyu Wang; Philippe Derreumaux
Journal: Chem Rev Date: 2015-03-19 Impact factor: 60.622

2. Symmetry-breaking transitions in the early steps of protein self-assembly.

Authors: Carmelo La Rosa; Marcello Condorelli; Giuseppe Compagnini; Fabio Lolicato; Danilo Milardi; Trang Nhu Do; Mikko Karttunen; Martina Pannuzzo; Ayyalusamy Ramamoorthy; Franca Fraternali; Francesca Collu; Human Rezaei; Birgit Strodel; Antonio Raudino
Journal: Eur Biophys J Date: 2020-03-02 Impact factor: 1.733

10. Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.

Authors: Srirupa Chakraborty; Payel Das
Journal: Sci Rep Date: 2017-08-30 Impact factor: 4.379

Early amyloid β-protein aggregation precedes conformational change.

Review 1. Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.

2. Symmetry-breaking transitions in the early steps of protein self-assembly.

3. Monomer Dynamics of Alzheimer Peptides and Kinetic Control of Early Aggregation in Alzheimer's Disease.

4. Comparing the Aggregation Free Energy Landscapes of Amyloid Beta(1-42) and Amyloid Beta(1-40).

5. αB-Crystallin Chaperone Inhibits Aβ Aggregation by Capping the β-Sheet-Rich Oligomers and Fibrils.

6. Visualizing and trapping transient oligomers in amyloid assembly pathways.

7. Study of structural stability and damaging effect on membrane for four Aβ42 dimers.

8. Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution.

9. Influence of Hyperglycemic Conditions on Self-Association of the Alzheimer's Amyloid β (Aβ_1-42) Peptide.

10. Emergence of Alternative Structures in Amyloid Beta 1-42 Monomeric Landscape by N-terminal Hexapeptide Amyloid Inhibitors.