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10.1039/c7cp02849k http://scihub22266oqcxt.onion/10.1039/c7cp02849k C5654640!5654640!28671211     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Phys+Chem+Chem+Phys 2017 ; 19 (27): 18036-46 Nephropedia Template TP {{tp|p=28671211|t=2017. Glucose Directs Amyloid-beta Into Membrane-Active Oligomers |pdf=|usr=}}{{28671211}} gab.com Text Glucose Directs Amyloid-beta Into Membrane-Active Oligomers JO: Phys Chem Chem Phys http://www.kidney.de/pget.php?&tw=1&pmid=28671211 #FOAvip Oligomeric Amyloid-? 1?42 (A?-42) peptides are considered to be the most toxic species connected to the occurrence of Alzheimer?s disease. However, not all aggregation conditions promote oligomer formation in vitro, raising the question whether oligomer formation in vivo also requires a specific suitable cellular environment. We recently found that interaction with neuronal membranes initiates aggregation of A?-42 and neuronal uptake. Our data suggest that small molecules in the extracellular space can facilitate the formation of membrane-active A?-42 oligomers. We analyzed the early stage of A?-42 aggregation in the presence of glucose and sucrose and found that these sugars strongly favor A?-42 oligomer formation. We characterized oligomers by dynamic light scattering, atomic force microscopy, immuno-transmission electron microscopy and fluorescence cross correlation spectroscopy. We found that A?-42 spontaneously and rapidly forms low molecular weight oligomers in the presence of sugars. Slightly acidic pH (6.7?7) greatly favors oligomer formation when compared to the extracellular physiological pH (7.4). Circular dichroism demonstrated that in presence of crowding agents A?-42 oligomers did not adopt a ?-sheet structure. Unstructured oligomeric A?-42 interacted with membrane bilayers of giant unilamellar vesicles (GUV) and neuronal model cells, facilitated cellular uptake of A?-42, and inhibition of mitochondrial activity. Our data therefore suggest that elevated concentrations of glucose within the range observed in diabetic individuals (10 mM) facilitate the formation of membrane-active A?-42 oligomers. Twit Text FOAVip Glucose Directs Amyloid-beta Into Membrane-Active Oligomers ????Phys Chem Chem Phys http://www.kidney.de/pget.php?&tw=1&pmid=28671211 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28671211 #FOAvip English Wikipedia <ref>{{Cite pmid|28671211}}</ref> Glucose Directs Amyloid-beta Into Membrane-Active Oligomers #MMPMID28671211 Kedia N; Almisry M; Bieschke J Phys Chem Chem Phys 2017[Jul]; 19 (27): 18036-46 PMID28671211show ga Oligomeric Amyloid-? 1?42 (A?-42) peptides are considered to be the most toxic species connected to the occurrence of Alzheimer?s disease. However, not all aggregation conditions promote oligomer formation in vitro, raising the question whether oligomer formation in vivo also requires a specific suitable cellular environment. We recently found that interaction with neuronal membranes initiates aggregation of A?-42 and neuronal uptake. Our data suggest that small molecules in the extracellular space can facilitate the formation of membrane-active A?-42 oligomers. We analyzed the early stage of A?-42 aggregation in the presence of glucose and sucrose and found that these sugars strongly favor A?-42 oligomer formation. We characterized oligomers by dynamic light scattering, atomic force microscopy, immuno-transmission electron microscopy and fluorescence cross correlation spectroscopy. We found that A?-42 spontaneously and rapidly forms low molecular weight oligomers in the presence of sugars. Slightly acidic pH (6.7?7) greatly favors oligomer formation when compared to the extracellular physiological pH (7.4). Circular dichroism demonstrated that in presence of crowding agents A?-42 oligomers did not adopt a ?-sheet structure. Unstructured oligomeric A?-42 interacted with membrane bilayers of giant unilamellar vesicles (GUV) and neuronal model cells, facilitated cellular uptake of A?-42, and inhibition of mitochondrial activity. Our data therefore suggest that elevated concentrations of glucose within the range observed in diabetic individuals (10 mM) facilitate the formation of membrane-active A?-42 oligomers. äGlucose Directs Amyloid-beta Into Membrane-Active Oligomers (epmc).pdf DeepDyve Pubget Overpricing