Membrane effects of lysozyme amyloid fibrils

Anna Kastorna; Valeriya Trusova; Galyna Gorbenko; Paavo Kinnunen

doi:10.1016/j.chemphyslip.2012.02.002

Membrane effects of lysozyme amyloid fibrils

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

^*Corresponding author for this work

V. N. Karazin Kharkiv National University

Research output: Contribution to journal › Article › Scientific › peer-review

19 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 language	English
Pages (from-to)	331-337
Number of pages	7
Journal	Chemistry and Physics of Lipids
Volume	165
Issue number	3
DOIs	https://doi.org/10.1016/j.chemphyslip.2012.02.002
Publication status	Published - Apr 2012
MoE publication type	A1 Journal article-refereed

Keywords

Fluorescent probes
Lipid packing
Lysozyme fibrils
Membrane hydration

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10.1016/j.chemphyslip.2012.02.002

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title = "Membrane effects of lysozyme amyloid fibrils",

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.",

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author = "Anna Kastorna and Valeriya Trusova and Galyna Gorbenko and Paavo Kinnunen",

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T1 - Membrane effects of lysozyme amyloid fibrils

AU - Kastorna, Anna

AU - Trusova, Valeriya

AU - Gorbenko, Galyna

AU - Kinnunen, Paavo

PY - 2012/4

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N2 - 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.

AB - 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.

KW - Fluorescent probes

KW - Lipid packing

KW - Lysozyme fibrils

KW - Membrane hydration

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DO - 10.1016/j.chemphyslip.2012.02.002

M3 - Article

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EP - 337

JO - Chemistry and Physics of Lipids

JF - Chemistry and Physics of Lipids

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Membrane effects of lysozyme amyloid fibrils

Abstract

Keywords

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