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Interactions of Lipid Membranes with Fibrillar Protein Aggregates

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Lipids in Protein Misfolding

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 855))

Abstract

Amyloid fibrils are an intriguing class of protein aggregates with distinct physicochemical, structural and morphological properties. They display peculiar membrane-binding behavior, thus adding complexity to the problem of protein-lipid interactions. The consensus that emerged during the past decade is that amyloid cytotoxicity arises from a continuum of cross-β-sheet assemblies including mature fibrils. Based on literature survey and our own data, in this chapter we address several aspects of fibril-lipid interactions, including (i) the effects of amyloid assemblies on molecular organization of lipid bilayer; (ii) competition between fibrillar and monomeric membrane-associating proteins for binding to the lipid surface; and (iii) the effects of lipids on the structural morphology of fibrillar aggregates. To illustrate some of the processes occurring in fibril-lipid systems, we present and analyze fluorescence data reporting on lipid bilayer interactions with fibrillar lysozyme and with the N-terminal 83-residue fragment of amyloidogenic mutant apolipoprotein A-I, 1-83/G26R/W@8. The results help understand possible mechanisms of interaction and mutual remodeling of amyloid fibers and lipid membranes, which may contribute to amyloid cytotoxicity.

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Abbreviations

1-83/G26R/W@8:

N-terminal 1-83 fragment of apoA-I with G26R mutation

AFM:

Atomic force microscopy

apoA-I:

Apolipoprotein A-I

AV-PC:

Anthrylvinyl-labeled PC

Aβ:

Amyloid-β peptide

Chol:

Cholesterol

CL:

Cardiolipin

cyt c :

Cytochrome c

FRET:

Förster resonance energy transfer

GP:

Generalized fluorescence polarization of Laurdan

HR:

Helical ribbon

PC:

Phosphatidylcholine

PG:

Phosphatidylglycerol

PS:

Phosphatidylserine

ThT:

Thioflavin T

TR:

Twisted ribbon

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Acknowledgements

The authors thank Prof. Kenichi Akaji and Dr. Hiroyuki Kawashima (Kyoto Pharmaceutical University) for their help with AFM, and Dr. Rohit Sood (Aalto University) for his aid with transmission electron microscopy. This work was supported by the grant from Fundamental Research State Fund of Ukraine (project number F54.4/015 to G. G.) and Grant-in-Aid for Scientific Research 25293006 (to H. S.) from the Japan Society for the Promotion of Science.

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Authors and Affiliations

  1. Department of Nuclear and Medical Physics, V.N. Karazin Kharkiv National University, 4 Svobody Sq., Kharkov, 61077, Ukraine

    Galyna Gorbenko, Valeriya Trusova & Mykhailo Girych

  2. Institute of Health Biosciences, Graduate School of Pharmaceutical Sciences, The University of Tokushima, 1-78-1 Shomachi, Tokushima, 770-8505, Japan

    Emi Adachi, Chiharu Mizuguchi & Hiroyuki Saito

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  1. Galyna Gorbenko
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  2. Valeriya Trusova
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  3. Mykhailo Girych
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  4. Emi Adachi
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  6. Hiroyuki Saito
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Correspondence to Galyna Gorbenko .

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  1. Dept. of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts, USA

    Olga Gursky

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Gorbenko, G., Trusova, V., Girych, M., Adachi, E., Mizuguchi, C., Saito, H. (2015). Interactions of Lipid Membranes with Fibrillar Protein Aggregates. In: Gursky, O. (eds) Lipids in Protein Misfolding. Advances in Experimental Medicine and Biology, vol 855. Springer, Cham. https://doi.org/10.1007/978-3-319-17344-3_6

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