Effect of copper (II) ion against elongation behavior of amyloid β fibrils on liposome membranes

Shimanouchi, Toshinori; Onishi, Ryo; Kitaura, Nachi; Umakoshi, Hiroshi; Kuboi, Ryoichi

doi:10.1002/crat.201100344

Cited by 4 publications

(5 citation statements)

References 37 publications

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“…I) Initial period is characterized by no obvious change of resistance during the first 8 h. The result indicates that little interaction occurs between Aβ(1–40) and the PC membranes. Accumulating evidences show that monomeric Aβ is nontoxic and hardly interacts with PC membranes at neutral pH . It may be because the interactions between Aβ and membranes with zwitterionic lipid surfaces are mainly dominated by hydrophobic interactions as mentioned in the section of introduction, however Aβ monomers have little hydrophobicity to interact with the membranes .…”

Section: Resultsmentioning

confidence: 99%

A Cantilever‐based Biosensor for Real‐time Monitoring of Interactions between Amyloid‐β(1–40) and Membranes Comprised of Phosphatidylcholine Lipids with Different Hydrophobic Acyl Chains

et al. 2016

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Accumulating evidence suggests that interaction between amyloid‐β (Aβ) and cell membrane is crucial to the pathogenesis of Alzheimer's disease (AD), and thus an increasing understanding of the impact of membrane composition on Aβ‐membrane interaction becomes essential for the mechanism elucidation of Aβ‐membrane interaction and the early diagnosis of AD. In this work, electrically neutral phosphatidylcholine (PC) as the most major class of membrane phospholipids, including 1,2‐dipalmitoyl‐sn‐glycero‐3‐phosphocholine (DPPC), 1,2‐distearoyl‐sn‐glycero‐3‐phosphocholine (DSPC), 1‐palmitoyl‐2‐oleoyl‐sn‐glycero‐3‐phosphocholine (POPC), and Aβ(1–40) as the most common amyloid protein were selected as the research subjects, and a developed cantilever‐based biosensor, on which liposomes comprised of PC lipids were immobilized, was applied to characterize in real time the interactions between Aβ(1–40) and membranes comprised of PC lipids with different hydrophobic acyl chains, and to evaluate the effect of cholesterol incorporated in membrane on Aβ‐membrane interaction during the whole process of Aβ(1–40) fibrillization. The results illustrate that the interaction between Aβ(1–40) and PC membrane can be divided into three stages, which are related to the change in molecular states of Aβ. More importantly, it is found that membranes comprised of PC lipids with shorter saturated acyl chains show higher interaction ability with Aβ(1–40), and the incorporation of cholesterol into PC bilayer can remarkably accelerate and strengthen Aβ(1–40)‐membrane interaction. These results confirm that hydrophobicity is the main driving force for the interactions between Aβ(1–40) and PC membranes. In return, the above results enlightened us to apply the current micro‐cantilever immobilized with cholesterol‐containing DPPC liposomes to challenge the detection of low‐concentration Aβ(1–40). This time 50‐nM Aβ(1–40) in aqueous solution has been effectively detected, suggesting that this proposed detection technique would contribute to Aβ detection and early diagnosis of AD in the future.

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Section: Resultsmentioning

confidence: 99%

A Cantilever‐based Biosensor for Real‐time Monitoring of Interactions between Amyloid‐β(1–40) and Membranes Comprised of Phosphatidylcholine Lipids with Different Hydrophobic Acyl Chains

et al. 2016

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“…The authors observed the ability of Cu 2+ to inhibit the fibrils’ growth in a bulk aqueous solution. However, the presence of the membrane model attenuated this inhibitory effect [51] . Specifically, they found that Cu 2+ inhibits the nucleation phase, leading to the formation of Aβ/Cu complexes, which are inactive to the fibrils’ growth.…”

Section: Factors Modulating Aβ‐lipid Membrane Interactionsmentioning

confidence: 99%

“…Shimanouchi et al . (2011) [50–51] investigated the copper (Cu 2+ )‐mediated growth of Aβ 1–40 fibrils in absence and presence of oxidized and negatively charged LUVs. The authors observed the ability of Cu 2+ to inhibit the fibrils’ growth in a bulk aqueous solution.…”

Section: Factors Modulating Aβ‐lipid Membrane Interactionsmentioning

confidence: 99%

The Role of Amyloid β‐Biomembrane Interactions in the Pathogenesis of Alzheimer's Disease: Insights from Liposomes as Membrane Models

2021

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The aggregation and deposition of amyloid β (Aβ) peptide onto neuronal cells, with consequent cellular membrane perturbation, are central to the pathogenesis of Alzheimer's disease (AD). Substantial evidence reveals that biological membranes play a key role in this process. Thus, elucidating the mechanisms by which Aβ interacts with biomembranes and becomes neurotoxic is fundamental to developing effective therapies for this devastating progressive disease. However, the structural basis behind such interactions is not fully understood, largely due to the complexity of natural membranes. In this context, lipid biomembrane models provide a simplified way to mimic the characteristics and composition of membranes. Aβ‐biomembrane interactions have been extensively investigated applying artificial membrane models to elucidate the molecular mechanisms underlying the AD pathogenesis. This review summarizes the latest findings on this field using liposomes as biomembrane model, as they are considered the most promising 3D model. The current challenges and future directions are discussed.

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“…Subsequently, Shimanouchi and co-workers first observed the growth behavior of Aβ fibrils in the presence of liposomes and metal ion (copper(II) ion). The influences of those additives on the growth behavior of amyloid fibrils were also quantitatively investigated to estimate the inhibitory effect . The result of this work indicated that copper(II) ion showed the strong inhibitory effect on the growth of Aβ fibrils in a bulk aqueous solution.…”

Section: Experimental Research Progressmentioning

confidence: 99%

“…The influences of those additives on the growth behavior of amyloid fibrils were also quantitatively investigated to estimate the inhibitory effect. 38 The result of this work indicated that copper(II) ion showed the strong inhibitory effect on the growth of Aβ fibrils in a bulk aqueous solution. Successively, Lovas and co-workers combined AFM and Molecular Dynamics (MD) simulations for characterizing the misfolding process of an Aβ peptide.…”

Section: Experimental Research Progressmentioning

confidence: 99%

Characterization of Recognition Events between Proteins on a Single Molecule Level with Atomic Force Microscopy

Xie

Wang

Feng

2016

Ind. Eng. Chem. Res.

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The application of functional imaging tools and techniques on the molecular level enables investigators to characterize structures of biomolecules and interactions between biomolecules. The characterization of recognition events between biomolecules with atomic force microscopy (AFM) is a new methodology in biological research. Recent advances in the field of scanning probe microscopy especially atomic force microscopy have made it possible to discover the dynamic systems of molecular self-assembly and quantify the molecular forces between proteins. The interaction mechanisms between biomolecules were explored by many researchers to tackle broad-category initiatives of human diseases. This review overviews the advances in characterizing recognition events between proteins on the molecular level, specifically on antigen−antibody interactions and the aggregation of amyloid-β peptides. AFM as an emerging approach for characterizing biomolecular interactions will also be highlighted. Furthermore, the potential and limitations of AFM for the measurement of single molecule interactions and the issues in analysis procedure will be discussed.

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Effect of copper (II) ion against elongation behavior of amyloid β fibrils on liposome membranes

Cited by 4 publications

References 37 publications

A Cantilever‐based Biosensor for Real‐time Monitoring of Interactions between Amyloid‐β(1–40) and Membranes Comprised of Phosphatidylcholine Lipids with Different Hydrophobic Acyl Chains

A Cantilever‐based Biosensor for Real‐time Monitoring of Interactions between Amyloid‐β(1–40) and Membranes Comprised of Phosphatidylcholine Lipids with Different Hydrophobic Acyl Chains

The Role of Amyloid β‐Biomembrane Interactions in the Pathogenesis of Alzheimer's Disease: Insights from Liposomes as Membrane Models

Characterization of Recognition Events between Proteins on a Single Molecule Level with Atomic Force Microscopy

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