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

^*Tämän työn vastaava kirjoittaja

V. N. Karazin Kharkiv National University

Tutkimustuotos: Lehtiartikkeli › Article › Scientific › vertaisarvioitu

19 Sitaatiot (Scopus)

Abstrakti

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.

Alkuperäiskieli	Englanti
Sivut	331-337
Sivumäärä	7
Julkaisu	Chemistry and Physics of Lipids
Vuosikerta	165
Numero	3
DOI - pysyväislinkit	https://doi.org/10.1016/j.chemphyslip.2012.02.002
Tila	Julkaistu - huhtik. 2012
OKM-julkaisutyyppi	A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä

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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.",

keywords = "Fluorescent probes, Lipid packing, Lysozyme fibrils, Membrane hydration",

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

year = "2012",

month = apr,

doi = "10.1016/j.chemphyslip.2012.02.002",

language = "English",

volume = "165",

pages = "331--337",

journal = "Chemistry and Physics of Lipids",

issn = "0009-3084",

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TY - JOUR

T1 - Membrane effects of lysozyme amyloid fibrils

AU - Kastorna, Anna

AU - Trusova, Valeriya

AU - Gorbenko, Galyna

AU - Kinnunen, Paavo

PY - 2012/4

Y1 - 2012/4

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

UR - http://www.scopus.com/inward/record.url?scp=84858716890&partnerID=8YFLogxK

U2 - 10.1016/j.chemphyslip.2012.02.002

DO - 10.1016/j.chemphyslip.2012.02.002

M3 - Article

C2 - 22406142

AN - SCOPUS:84858716890

SN - 0009-3084

VL - 165

SP - 331

EP - 337

JO - Chemistry and Physics of Lipids

JF - Chemistry and Physics of Lipids

IS - 3

ER -

Membrane effects of lysozyme amyloid fibrils

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