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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kukol, Andreas Strodel, Birgit Poojari, Chetan |
| Description | Author Affiliation: Poojari C ( Research Centre Jülich, Institute of Complex Systems: Structural Biochemistry, 52425 Jülich, Germany.) |
| Abstract | The etiology of Alzheimer's disease is thought to be linked to interactions between amyloid-β (Aβ) and neural cell membranes, causing membrane disruption and increased ion conductance. The effects of Aβ on lipid behavior have been characterized experimentally, but structural and causal details are lacking. We used atomistic molecular dynamics simulations totaling over 6 μs in simulation time to investigate the behavior of $Aβ_{42}$ in zwitterionic and anionic lipid bilayers. We simulated transmembrane β-sheets (monomer and tetramer) resulting from a global optimization study and a helical structure obtained from an NMR study. In all simulations $Aβ_{42}$ remained embedded in the bilayer. It was found that the surface charge and the lipid tail type are determinants for transmembrane stability of $Aβ_{42}$ with zwitterionic surfaces and unsaturated lipids promoting stability. From the considered structures, the β-sheet tetramer is most stable as a result of interpeptide interactions. We performed an in-depth analysis of the translocation of water in the $Aβ_{42}-bilayer$ systems. We observed that this process is generally fast (within a few nanoseconds) yet generally slower than in the peptide-free bilayers. It is mainly governed by the lipid type, simulation temperature and $Aβ_{42}$ conformation. The rate limiting step is the permeation through the hydrophobic core, where interactions between $Aβ_{42}$ and permeating $H_{2}O$ molecules slow the translocation process. The β-sheet tetramer allows more water molecules to pass through the bilayer compared to monomeric Aβ, allowing us to conclude that the experimentally observed permeabilization of membranes must be due to membrane-bound Aβ oligomers, and not monomers. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 2 |
| Volume Number | 1828 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2013-02-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Alzheimer Disease Metabolism Amyloid Beta-Peptides Chemistry Cell Membrane 1,2-Dipalmitoylphosphatidylcholine Algorithms Computer Simulation Hydrogen-Ion Concentration Ions Lipid Bilayers Lipids Magnetic Resonance Spectroscopy Peptides Phosphatidylcholines Phosphatidylglycerols Protein Structure, Secondary Temperature Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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