Titlebook: Lipids in Protein Misfolding; Olga Gursky Book 2015 The Editor(s) (if applicable) and The Author(s), under exclusive license to Springer N

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Role of Lipids in Folding, Misfolding and Function of Integral Membrane Proteins, similarity. Furthermore, the atomic structures of the same protein in different lipid environments are also very similar. This suggests that certain stable folds optimized for a specific function have been selected by evolution. On the other hand, there is growing evidence that, despite the overall

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,Lipids in Amyloid-β Processing, Aggregation, and Toxicity,actor for AD. Aβ is an amphiphilic peptide that interacts with various lipids, proteins and their assemblies, which can lead to variation in Aβ aggregation in vitro and in vivo. Upon interaction with the lipid raft components, such as cholesterol, gangliosides and phospholipids, Aβ can aggregate on

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Intrinsic Stability, Oligomerization, and Amyloidogenicity of HDL-Free Serum Amyloid A,ibrils in vitro at 37 °C whereas pathogenic mSAA1.1 has a long lag (nucleation) phase, and eventually forms fibrils of different morphology than mSAA2.2. Remarkably, human SAA1.1 does not form mature fibrils in vitro. Thus, it appears that the intrinsic amyloidogenicity of SAA is not a key determina

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Interactions of Lipid Membranes with Fibrillar Protein Aggregates,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

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