Abstract
The binding of monomeric and aggregated variants of 1–83 N-terminal fragment of apolipoprotein A-I with substitution mutations G26R, G26R/W@8, G26R/W@50 and G26R/W@72 to the model lipid membranes composed of phosphatidylcholine and its mixture with cholesterol has been investigated using fluorescent probes pyrene and Laurdan. Examination of pyrene spectral behavior did not reveal any marked influence of apoA-I mutants on the hydrocarbon region of lipid bilayer. In contrast, probing the membrane effects by Laurdan revealed decrease in the probe generalized polarization in the presence of aggregated proteins. suggesting that oligomeric and fibrillar apoA-I species induce increase in hydration degree and reduction of lipid packing density in the membrane interfacial region. These findings may shed light on molecular details of amyloid cytotoxicity.
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This work was supported by the grant from Fundamental Research State Fund of Ukraine (project number F54.4/015) and Grant-in-Aid for Scientific Research 25293006 (to H.S.) from the Japan Society for the Promotion of Science.
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Trusova, V., Gorbenko, G., Girych, M. et al. Membrane Effects of N-Terminal Fragment of Apolipoprotein A-I: A Fluorescent Probe Study. J Fluoresc 25, 253–261 (2015). https://doi.org/10.1007/s10895-015-1501-9
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DOI: https://doi.org/10.1007/s10895-015-1501-9