FATAFTA, H., C. POOJARI, A. SAYYED-AHMAD, B. STRODEL a Michael Christopher OWEN. Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes. ACS CHEMICAL NEUROSCIENCE. WASHINGTON: AMER CHEMICAL SOC, 2020, roč. 11, č. 4, s. 535-548, 27 s. ISSN 1948-7193. Dostupné z: https://dx.doi.org/10.1021/acschemneuro.9b00558. |
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@article{1750456, author = {Fatafta, H. and Poojari, C. and SayyedandAhmad, A. and Strodel, B. and Owen, Michael Christopher}, article_location = {WASHINGTON}, article_number = {4}, doi = {http://dx.doi.org/10.1021/acschemneuro.9b00558}, keywords = {Amyloid-beta peptide; molecular dynamics; membrane simulations; oxidative stress; GM1; peptide membrane interactions}, language = {eng}, issn = {1948-7193}, journal = {ACS CHEMICAL NEUROSCIENCE}, title = {Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes}, url = {https://pubs.acs.org/doi/10.1021/acschemneuro.9b00558}, volume = {11}, year = {2020} }
TY - JOUR ID - 1750456 AU - Fatafta, H. - Poojari, C. - Sayyed-Ahmad, A. - Strodel, B. - Owen, Michael Christopher PY - 2020 TI - Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes JF - ACS CHEMICAL NEUROSCIENCE VL - 11 IS - 4 SP - 535-548 EP - 535-548 PB - AMER CHEMICAL SOC SN - 19487193 KW - Amyloid-beta peptide KW - molecular dynamics KW - membrane simulations KW - oxidative stress KW - GM1 KW - peptide membrane interactions UR - https://pubs.acs.org/doi/10.1021/acschemneuro.9b00558 N2 - Oxidative stress is known to play an important role in the pathogenesis of Alzheimer's disease. Moreover, it is becoming increasingly evident that the plasma membrane of neurons plays a role in modulating the aggregation and toxicity of Alzheimer's amyloid-beta peptide (A beta). In this study, the combined and interdependent effects of oxidation and membrane interactions on the 42 residues long A beta isoform are investigated using molecular simulations. Hamiltonian replica exchange molecular dynamics simulations are utilized to elucidate the impact of selected oxidized glycine residues of A beta 42 on the interactions of the peptide with a model membrane comprised of 70% POPC, 25% cholesterol, and 5% of the ganglioside GM1. The main findings are that, independent of the oxidation state, A beta prefers binding to GM1 over POPC, which is further enhanced by the oxidation of Gly29 and Gly33 and reduced the formation of beta-sheet. Our results suggest that the differences observed in A beta 42 conformations and its interaction with a lipid bilayer upon oxidation originate from the position of the oxidized Gly residue with respect to the hydrophobic sequence of A beta 42 involving the Gly29-XXX-Gly33-XXX-Gly37 motif and from specific interactions between the peptide and the terminal sugar groups of GM1. ER -
FATAFTA, H., C. POOJARI, A. SAYYED-AHMAD, B. STRODEL a Michael Christopher OWEN. Role of Oxidized Gly25, Gly29, and Gly33 Residues on the Interactions of A beta(1-42) with Lipid Membranes. \textit{ACS CHEMICAL NEUROSCIENCE}. WASHINGTON: AMER CHEMICAL SOC, 2020, roč.~11, č.~4, s.~535-548, 27 s. ISSN~1948-7193. Dostupné z: https://dx.doi.org/10.1021/acschemneuro.9b00558.
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