Membrane Effects of N-Terminal Fragment of Apolipoprotein A-I: A Fluorescent Probe Study
| Autor: | Chiharu Mizuguchi, Hiroyuki Saito, Galyna Gorbenko, Paavo K.J. Kinnunen, Mykhailo Girych, Rohit Sood, Valeriya Trusova, Emi Adachi |
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| Rok vydání: | 2015 |
| Předmět: |
Amyloid
Sociology and Political Science Apolipoprotein B Lipid Bilayers Molecular Sequence Data Clinical Biochemistry Biochemistry chemistry.chemical_compound 2-Naphthylamine Phosphatidylcholine Humans Amino Acid Sequence Lipid bilayer Spectroscopy Fluorescent Dyes Pyrenes Apolipoprotein A-I biology Chemistry Cholesterol Cell Membrane Fluorescence Peptide Fragments Clinical Psychology Membrane Mutation Phosphatidylcholines biology.protein Pyrene lipids (amino acids peptides and proteins) Protein Multimerization Laurdan Law Laurates Social Sciences (miscellaneous) |
| Zdroj: | Journal of Fluorescence. 25:253-261 |
| ISSN: | 1573-4994 1053-0509 |
| DOI: | 10.1007/s10895-015-1501-9 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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