Membrane effects of lysozyme amyloid fibrils

Anna Kastorna*, Valeriya Trusova, Galyna Gorbenko, Paavo Kinnunen

*Corresponding author for this work

    Research output: Contribution to journalArticleScientificpeer-review

    16 Citations (Scopus)

    Abstract

    The influence of mature lysozyme fibrils on the structural and physical properties of model membranes composed of phosphatidylcholine (PC) and its mixtures with cardiolipin (CL) (10 mol%) and cholesterol (Chol) (30 mol%) was studied using fluorescent probes DPH, pyrene, Laurdan and MBA. Analysis of pyrene fluorescence spectra along with the measurements of DPH fluorescence anisotropy revealed that the structure of hydrocarbon chains region of lipid bilayer is not affected by the fibrillar aggregates of lysozyme. In contrast, probing the membrane effects by Laurdan and MBA showed the rise of both the generalized polarization of Laurdan and the MBA fluorescence anisotropy, suggesting that amyloid protein induces reduction of bilayer hydration and increase of lipid packing in the interfacial region of model membranes.

    Original languageEnglish
    Pages (from-to)331-337
    Number of pages7
    JournalChemistry and Physics of Lipids
    Volume165
    Issue number3
    DOIs
    Publication statusPublished - Apr 2012
    MoE publication typeA1 Journal article-refereed

    Keywords

    • Fluorescent probes
    • Lipid packing
    • Lysozyme fibrils
    • Membrane hydration

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