Influence of amyloid-β peptides with different lengths and amino acid sequences on the lateral diffusion of lipids in model membranes

Buchsteiner, A.; Hauß, Thomas; Dencher, Norbert A.

doi:10.1039/c1sm06823g

Cited by 15 publications

(18 citation statements)

References 22 publications

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“…502 The influence of A (25-35) and A (22-40) on the picosecond dynamics of lipid membranes has been examined by quasi-elastic neutron scattering. 503 The main influence was on long-range translational diffusion, although localized diffusion was also considered. By selection of the A (11-22) fragment, the role of charge, and the influence of pH, in governing the interaction of A with lipids was examined.…”

Section: Interactions With Lipid Membranesmentioning

confidence: 99%

The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization

2012

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Section: Interactions With Lipid Membranesmentioning

confidence: 99%

The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization

2012

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“…There is strong evidence that fragments of this peptide interact with lipid membranes, altering membrane structure [ 9 , 10 ], dynamics [ 11 , 12 ] and membrane function [ 13 ], thereby leading to changes in membrane permeability [ 14 ] and pore formation [ 15 ], although the exact mechanism remains obscure [ 16 ].…”

Section: Introductionmentioning

confidence: 99%

“…While Aβ peptides are frequently reported in an extracellular location, A

and A

molecules were found to strongly interact with negatively charged lipids and to bind to anionic, negatively charged membranes [ 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 ], orienting parallel to the membrane surface. Studies on fragments of the amyloid-β peptide have shown that the peptide interacts with negatively charged membranes, entering the membrane and modifying membrane lipid dynamics [ 11 , 12 ]. The short, primarily hydrophobic (25–35) amino acid fragment embeds itself into the hydrophobic core of the membrane, and longer (1–40) or (1–42) peptides react in a similar way [ 38 , 39 , 40 , 41 , 42 ].…”

Section: Introductionmentioning

confidence: 99%

The Position of Aβ22-40 and Aβ1-42 in Anionic Lipid Membranes Containing Cholesterol

et al. 2015

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Amyloid-β peptides interact with cell membranes in the human brain and are associated with neurodegenerative diseases, such as Alzheimer’s disease. An emerging explanation of the molecular mechanism, which results in neurodegeneration, places the cause of neurotoxicity of the amyloid-β peptides on their potentially negative interaction with neuronal membranes. It is known that amyloid-β peptides interact with the membrane, modifying the membrane’s structural and dynamic properties. We present a series of X-ray diffraction experiments on anionic model lipid membranes containing various amounts of cholesterol. These experiments provide experimental evidence for an interaction of both the full length amyloid-β1−42 peptide, and the peptide fragment amyloid-β22−40 with anionic bilayer containing cholesterol. The location of the amyloid-β peptides was determined from these experiments, with the full length peptide embedding into the membrane, and the peptide fragment occupying 2 positions—on the membrane surface and embedded into the membrane core.

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“…They have detected two populations of the peptide, one in the aqueous phase close to the vesicle surface and the other population intercalated deep inside the bilayer, with the C terminus close to the middle of the bilayer. Buchsteiner et al(2012,2010) have investigated the interaction of Aβ(25–35) with DMPC/DMPS model membranes by means of quasi-elastic neutron scattering. They have found that the Aβ(25–35) inserted in the bilayer affects the local dynamics of phospholipid molecules, as well as their lateral diffusion.…”

Section: Resultsmentioning

confidence: 99%

Interaction of the β amyloid – Aβ(25–35) – peptide with zwitterionic and negatively charged vesicles with and without cholesterol

Singh

Perić

2018

Chemistry and Physics of Lipids

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The interactions of the Alzheimer’s β-amyloid peptide, Aβ(25–35), with 18:1 (Δ9-Cis) PC 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), L-α-phosphatidylcholine (EPC), 1,2-dioleoyl-sn-glycero-3-phospho-(1’-rac-glycerol) (sodium salt) (DOPG), and L-α-phosphatidylglycerol (EPG) phospholipid vesicles with and without cholesterol (Ch) are studied by the nitroxide spin probe electron paramagnetic resonance (EPR) method. Two nitroxide spin probes, 2,2,6,6-tetramethyl-piperidin-1-oxyl-4-yl hexadecanoate (TP, TEMPO-Palmitate) and 2-Ethyl-2-(15-methoxy-15-oxopentadecyl)-4,4-dimethyl-3-oxazolidinyloxy (16-DSE), are utilized in the study. TEMPO-Palmitate has the reporting EPR moiety located at the top of this spin probe, while 16-DSE has the reporting EPR moiety located at the tail of the spin probe. These two probes enable us to sample the surface and the middle of the phospholipid bilayer, respectively. All EPR measurements are done above the melting points of all four phospholipids when the bilayer is in the liquid crystal phase, the physiologically relevant phase. Due to non-linear spectral line fitting, the EPR spectral parameters are extracted with high precision. The results show that there are two populations of Aβ(25–35) and that one of them is located in the hydrophobic phospholipid layer below the hydrophilic headgroup region. The second population appears to be weakly coupled to the surface of the bilayer. Both hydrophobic and electrostatic interactions affect the insertion of Aβ(25–35) in the bilayer. Also, there is strong evidence for an interaction between cholesterol and Aβ (25–35), which affects the dielectric and dynamic properties of the bilayer.

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Influence of amyloid-β peptides with different lengths and amino acid sequences on the lateral diffusion of lipids in model membranes

Cited by 15 publications

References 22 publications

The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization

The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization

The Position of Aβ22-40 and Aβ1-42 in Anionic Lipid Membranes Containing Cholesterol

Interaction of the β amyloid – Aβ(25–35) – peptide with zwitterionic and negatively charged vesicles with and without cholesterol

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