Chapter title |
Interactions of Lipid Membranes with Fibrillar Protein Aggregates
|
---|---|
Chapter number | 6 |
Book title |
Lipids in Protein Misfolding
|
Published in |
Advances in experimental medicine and biology, January 2015
|
DOI | 10.1007/978-3-319-17344-3_6 |
Pubmed ID | |
Book ISBNs |
978-3-31-917343-6, 978-3-31-917344-3
|
Authors |
Galyna Gorbenko, Valeriya Trusova, Mykhailo Girych, Emi Adachi, Chiharu Mizuguchi, Hiroyuki Saito, Gorbenko, Galyna, Trusova, Valeriya, Girych, Mykhailo, Adachi, Emi, Mizuguchi, Chiharu, Saito, Hiroyuki |
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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Demographic breakdown
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Unspecified | 1 | 9% |
Student > Master | 1 | 9% |
Other | 0 | 0% |
Unknown | 4 | 36% |
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Unspecified | 1 | 9% |
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Unknown | 4 | 36% |