Effect of amyloid beta peptides Aβ1–28 and Aβ25–40 on model lipid membranes

Йонов, Максим; Klajnert, Barbara; Gardikis, Κonstantinos; Hatziantoniou, Sophia; Pałecz, Bartłomiej; Salakhutdinov, B. A.; Cladera, Josep; Zamaraeva, Maria; Demetzos, Costas; Bryszewska, Maria

doi:10.1007/s10973-009-0405-9

Cited by 33 publications

(38 citation statements)

References 32 publications

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“…The behavior of the Aβ fragments in DMPC bilayer is consistent with the experimental data. 329 Similar trends were observed for Aβ interaction when studied in mixed bilayer. The Aβ 1-28 fragment fully enters the normal bilayer with high fraction of DHA and stays on the membrane surface of an AD bilayer.…”

Section: Amyloid β (Aβ) Peptidesupporting

confidence: 67%

Computer simulations of protein–membrane systems

Loschwitz

Olubiyi

Hub

et al. 2020

Computational Approaches for Understanding Dynamical Systems: Protein Folding and Assembly

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Section: Amyloid β (Aβ) Peptidesupporting

confidence: 67%

Computer simulations of protein–membrane systems

Loschwitz

Olubiyi

Hub

et al. 2020

Computational Approaches for Understanding Dynamical Systems: Protein Folding and Assembly

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“…The influence of membrane surface on the adsorption and aggregation of A β peptides have been investigated on solid surfaces, monolayer bilayers, self-assembled monolayers (SAMs), implicit membrane models, and models that mimic membrane structures [25–30]. The general observation is that solid surfaces promote the self-assembly of A β peptides.…”

Section: Aβ Adsorption and Insertion Mechanismmentioning

confidence: 99%

“…This is observed when the two fragments of A β 1–28 and A β 25–40 are incorporated into the bilayer. While the hydrophobic group of A β 25–40 is observed to locate inside the hydrophobic core region, A β 1–28 shows a greater propensity to interact with the hydrophilic region of the membrane [30]. In comparison to A β 1–28 , A β 25–40 is found to induce larger membrane perturbation and alteration.…”

Section: Aβ Adsorption and Insertion Mechanismmentioning

confidence: 99%

The Toxicity of Amyloid ß Oligomers

Zhao

Long

et al. 2012

IJMS

126

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In this review, we elucidate the mechanisms of A β oligomer toxicity which may contribute to Alzheimer’s disease (AD). In particular, we discuss on the interaction of A β oligomers with the membrane through the process of adsorption and insertion. Such interaction gives rises to phase transitions in the sub-structures of the A β peptide from α -helical to β -sheet structure. By means of a coarse-grained model, we exhibit the tendency of β -sheet structures to aggregate, thus providing further insights to the process of membrane induced aggregation. We show that the aggregated oligomer causes membrane invagination, which is a precursor to the formation of pore structures and ion channels. Other pathological progressions to AD due to A β oligomers are also covered, such as their interaction with the membrane receptors, and their direct versus indirect effects on oxidative stress and intraneuronal accumulation. We further illustrate that the molecule curcumin is a potential A β toxicity inhibitor as a β -sheet breaker by having a high propensity to interact with certain A β residues without binding to them. The comprehensive understanding gained from these current researches on the various toxicity mechanisms show promises in the provision of better therapeutics and treatment strategies in the near future.

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“…A method to load DCs with antigens is therefore urgently needed, since it requires an efficient carrier to deliver antigen across the plasma membrane. Different methods have so far included the use of liposomes, nanoparticles, polymeric micelles and nanogels [6][7][8][9][10][11][12][13]. In this context, dendrimers offer an alternative approach [14,15].…”

Section: Introductionmentioning

confidence: 99%