Amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes
Abstract The amyloid-beta peptide (Aβ) is considered a key factor in Alzheimer's disease (AD) ever since the discovery of the disease. The understanding of its damaging influence has however shifted recently from large fibrils observed in the inter-cellular environment to the small oligomers in...
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Nature Portfolio
2021
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oai:doaj.org-article:adfdcfbc3380435eb0ef46ee69ca3ce82021-11-14T12:23:05ZAmyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes10.1038/s41598-021-01347-72045-2322https://doaj.org/article/adfdcfbc3380435eb0ef46ee69ca3ce82021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-01347-7https://doaj.org/toc/2045-2322Abstract The amyloid-beta peptide (Aβ) is considered a key factor in Alzheimer's disease (AD) ever since the discovery of the disease. The understanding of its damaging influence has however shifted recently from large fibrils observed in the inter-cellular environment to the small oligomers interacting with a cell membrane. We studied the effect of temperature on the latter interactions by evaluating the structural characteristics of zwitterionic phosphatidylcholine (PC) membranes with incorporated Aβ25–35 peptide. By means of small angle neutron scattering (SANS), we have observed for the first time a spontaneous reformation of extruded unilamellar vesicles (EULVs) to discoidal bicelle-like structures (BLSs) and small unilamellar vesicles (SULVs). These changes in the membrane self-organization happen during the thermodynamic phase transitions of lipids and only in the presence of the peptide. We interpret the dramatic changes in the membrane's overall shape with parallel changes in its thickness as the Aβ25–35 triggered membrane damage and a consequent reorganization of its structure. The suggested process is consistent with an action of separate peptides or small size peptide oligomers rather than the result of large Aβ fibrils.Oleksandr IvankovTatiana N. MurugovaElena V. ErmakovaTomáš KondelaDina R. BadreevaPavol HrubovčákDmitry SoloviovAlexey TsarenkoAndrey RogachevAlexander I. KuklinNorbert KučerkaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021) |
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Medicine R Science Q Oleksandr Ivankov Tatiana N. Murugova Elena V. Ermakova Tomáš Kondela Dina R. Badreeva Pavol Hrubovčák Dmitry Soloviov Alexey Tsarenko Andrey Rogachev Alexander I. Kuklin Norbert Kučerka Amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes |
| description |
Abstract The amyloid-beta peptide (Aβ) is considered a key factor in Alzheimer's disease (AD) ever since the discovery of the disease. The understanding of its damaging influence has however shifted recently from large fibrils observed in the inter-cellular environment to the small oligomers interacting with a cell membrane. We studied the effect of temperature on the latter interactions by evaluating the structural characteristics of zwitterionic phosphatidylcholine (PC) membranes with incorporated Aβ25–35 peptide. By means of small angle neutron scattering (SANS), we have observed for the first time a spontaneous reformation of extruded unilamellar vesicles (EULVs) to discoidal bicelle-like structures (BLSs) and small unilamellar vesicles (SULVs). These changes in the membrane self-organization happen during the thermodynamic phase transitions of lipids and only in the presence of the peptide. We interpret the dramatic changes in the membrane's overall shape with parallel changes in its thickness as the Aβ25–35 triggered membrane damage and a consequent reorganization of its structure. The suggested process is consistent with an action of separate peptides or small size peptide oligomers rather than the result of large Aβ fibrils. |
| format |
article |
| author |
Oleksandr Ivankov Tatiana N. Murugova Elena V. Ermakova Tomáš Kondela Dina R. Badreeva Pavol Hrubovčák Dmitry Soloviov Alexey Tsarenko Andrey Rogachev Alexander I. Kuklin Norbert Kučerka |
| author_facet |
Oleksandr Ivankov Tatiana N. Murugova Elena V. Ermakova Tomáš Kondela Dina R. Badreeva Pavol Hrubovčák Dmitry Soloviov Alexey Tsarenko Andrey Rogachev Alexander I. Kuklin Norbert Kučerka |
| author_sort |
Oleksandr Ivankov |
| title |
Amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes |
| title_short |
Amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes |
| title_full |
Amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes |
| title_fullStr |
Amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes |
| title_full_unstemmed |
Amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes |
| title_sort |
amyloid-beta peptide (25–35) triggers a reorganization of lipid membranes driven by temperature changes |
| publisher |
Nature Portfolio |
| publishDate |
2021 |
| url |
https://doaj.org/article/adfdcfbc3380435eb0ef46ee69ca3ce8 |
| work_keys_str_mv |
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