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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lal, Ratnesh Arce, Fernando Teran Capone, Ricardo Jang, Hyunbum Ramachandran, Srinivasan Kotler, Samuel A. Nussinov, Ruth Kagan, Bruce L. Connelly, Laura |
| Description | Author Affiliation: Connelly L ( Department of Bioengineering, University of California, San Diego, La Jolla, California 92093, USA.) |
| Abstract | Alzheimer's disease (AD) is a protein misfolding disease characterized by a buildup of ß-amyloid (Aß) peptide as senile plaques, uncontrolled neurodegeneration, and memory loss. AD pathology is linked to the destabilization of cellular ionic homeostasis and involves Aß peptide-plasma membrane interactions. In principle, there are two possible ways through which disturbance of the ionic homeostasis can take place: directly, where the Aß peptide either inserts into the membrane and creates ion-conductive pores or destabilizes the membrane organization, or, indirectly, where the Aß peptide interacts with existing cell membrane receptors. To distinguish between these two possible types of Aß-membrane interactions, we took advantage of the biochemical tenet that ligand-receptor interactions are stereospecific; L-amino acid peptides, but not their D-counterparts, bind to cell membrane receptors. However, with respect to the ion channel-mediated mechanism, like L-amino acids, D-amino acid peptides will also form ion channel-like structures. Using atomic force microscopy (AFM), we imaged the structures of both D- and L-enantiomers of the full length Aß(1-42) when reconstituted in lipid bilayers. AFM imaging shows that both L- and D-Aß isomers form similar channel-like structures. Molecular dynamics (MD) simulations support the AFM imaged 3D structures. Previously, we have shown that D-Aß(1-42) channels conduct ions similarly to their L- counterparts. Taken together, our results support the direct mechanism of Aß ion channel-mediated destabilization of ionic homeostasis rather than the indirect mechanism through Aß interaction with membrane receptors. |
| ISSN | 15206106 |
| e-ISSN | 15205207 |
| Journal | The Journal of Physical Chemistry B |
| Issue Number | 5 |
| Volume Number | 116 |
| Language | English |
| Publisher | American Chemical Society (United States) |
| Publisher Date | 2012-02-09 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Alzheimer Disease Metabolism Amyloid Beta-Peptides Chemistry Ultrastructure Molecular Dynamics Simulation Peptide Fragments Amyloid Isomerism Lipid Bilayers Microscopy, Atomic Force Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Physical chemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Surfaces, Coatings and Films Materials Chemistry Medicine Physical and Theoretical Chemistry |
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