Controlling Amyloid‐β Peptide(1–42) Oligomerization and Toxicity by Fluorinated Nanoparticles

Saraiva, Ana M.; Cardoso, Isabel; Pereira, Maria do Carmo; Coelho, Manuel A. N.; Saraiva, Maria João; Möhwald, H.; Brezesinski, Gerald

doi:10.1002/cbic.201000237

Cited by 42 publications

(69 citation statements)

References 64 publications

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“…This study confirms the fibrillation‐inhibiting effect of charged micelles. Other charged nanoparticles (NPs) were shown to have also a fibrillation‐inhibiting effect . Liao et al .…”

Section: Discussionmentioning

confidence: 99%

“…Saraiva et al . demonstrated that fluorinated NPs promote an increase in the α‐helical content of the Aβ (1‐42) peptide and have an antioligomeric effect . Sulfonated and sulfated polystyrene NPs, which are negatively charged polymeric nanostructures, also affected the conformation of Aβ and induced an unordered state, delaying the peptide oligomerization .…”

Section: Discussionmentioning

confidence: 99%

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Charged surfactants induce a non‐fibrillar aggregation pathway of amyloid‐beta peptide

Loureiro

Rocha

Pereira

2013

Journal of Peptide Science

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The amyloid β-peptide with a sequence of 42 amino acids is the major constituent of extracellular amyloid deposits in Alzheimer's disease plaques. The control of the peptide self-assembly is difficult to achieve because the process is fast and is affected by many variables. In this paper, we describe the effect of different charged and non-charged surfactants on Aβ(₁₋₄₂) fibrillation to define common alternate aggregation pathways. The characterization of the peptide-surfactant interactions by ultra-structural analysis, thioflavin T assay and secondary structure analysis, suggested that charged surfactants interact with Aβ(₁₋₄₂) through electrostatic interactions. Charged micelles slow down the aggregation process and stabilize the peptide in the oligomeric state, whereas non-charged surfactants promote the Aβ(₁₋₄₂) fibril formation.

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“…This study confirms the fibrillation‐inhibiting effect of charged micelles. Other charged nanoparticles (NPs) were shown to have also a fibrillation‐inhibiting effect . Liao et al .…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Charged surfactants induce a non‐fibrillar aggregation pathway of amyloid‐beta peptide

Loureiro

Rocha

Pereira

2013

Journal of Peptide Science

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“…AD is the most common disease in the elderly population. To date, no effective treatment methods to AD have been given [5] . However, three approved treatments for AD should be directed toward decreasing Aβ production, increasing Aβ removal, and preventing Aβ fibril formation.…”

Section: Introductionmentioning

confidence: 99%

Studies on the interaction between vanillin and β-Amyloid protein via fluorescence spectroscopy and atomic force microscopy

Shi

Xue-wen

Zhou

et al. 2016

Chem. Res. Chin. Univ.

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β-Amyloid(Aβ) plaques and intracellular neurofibrillary lesions in the brain are markers of Alzheimer's disease(AD). The ability to safely decrease Aβ concentrations is potentially important as a preventive strategy for AD. The interactions between vanillin and Aβ polypeptide were investigated via fluorescence spectroscopy and atomic force microscopy(AFM). The results of fluorescence and synchronous spectroscopies illustrate that the intrinsic fluorescence of tyrosine(Tyr) residues in Aβ 1-42 aggregates can be quenched strongly upon the formation of vanillin-Aβ 1-42 complex. Thioflavine T(ThT)-induced fluorescence changes indicated that Aβ 1-42 aggregates could be disaggregated by vanillin, and the AFM images of Aβ 1-42 enunciated the depolymerization of Aβ 1-42 aggregates by vanillin in a dose-dependent manner. Vanillin may be a potential pharmacological agent for the treatment of AD.

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“…Also they can be able to interact with residues in their vicinity by exploiting the same intermolecular interaction as in Aβ assembly and disrupting the potential for further aggregation [148].…”

Section: Fluorine Incorporation Methodsmentioning

confidence: 99%

The Potential Effect of Fluorinated Compounds in the Treatment of Alzheimer’s Disease

Gomes¹,

Loureiro²,

Coelho³

et al. 2015

CPD

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Drug development for neurodegenerative diseases such as Alzheimer disease (AD) is a challenge not only due to the cellular molecular mechanisms involved but also because the inherent difficulty of most molecules to cross the blood-brain-barrier (BBB). To overcome these drawbacks, a promising approach is the development of fluorinated molecules and supramolecular assemblies.This review focus on the therapeutic potential of new fluorinated molecules developed as active and selective agents for AD to achieve the desired properties in terms of pharmacokinetic/pharmacodynamics and BBB targeting. The methods to fluorinate organic molecules are described and a brief characterization of the mechanisms of AD progression and therapeutic approaches are also addressed.The paradigm of cell biology knowledge and fluorine biochemistry is highlighted, such as organofluorine inhibitors of amyloid fibrilogenesis.

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Controlling Amyloid‐β Peptide(1–42) Oligomerization and Toxicity by Fluorinated Nanoparticles

Cited by 42 publications

References 64 publications

Charged surfactants induce a non‐fibrillar aggregation pathway of amyloid‐beta peptide

Charged surfactants induce a non‐fibrillar aggregation pathway of amyloid‐beta peptide

Studies on the interaction between vanillin and β-Amyloid protein via fluorescence spectroscopy and atomic force microscopy

The Potential Effect of Fluorinated Compounds in the Treatment of Alzheimer’s Disease

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