AFM and fluorescence spectrascopy investigation for disaggregation of existing Aβ fibrils by baicalein

Song, Sheng Mei; Wang, Yong Xiang; Xiong, Li Min; Qu, Ling Bo; Xu, Mao Tian

doi:10.1016/j.cclet.2012.03.001

Cited by 7 publications

(2 citation statements)

References 11 publications

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“…In recent years, more and more studies have been carried out to investigate the interaction between drug molecules and Aβ. Our previous studies [12,13] demonstrated that baicalein could disaggregate the existed Aβ fibrils. Song et al [14] proved that syringin from stem bark of Fraxinus rhynchophylla could provent neuronal cells from Aβ 25-35 -induced toxicity damage.…”

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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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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“…As shown from the atomic force microscopy (AFM) images, when Ab 42 is incubated with baicalein, the globular crystalloid aggregates of Ab 42 become smaller and long fibrils dissociate into globular deposits, highlighting the disaggregation effect of baicalein. 17 Another study by Wang and coworkers reported that baicalein rescued synaptic plasticity and memory loss in the AD mouse model. 18 Despite its noteworthy properties, the binding interactions of baicalein on Ab oligomers and the molecular mechanism of Ab fibril destabilization remain elusive.…”

Section: Introductionmentioning

confidence: 99%

Insights into the baicalein-induced destabilization of LS-shaped Aβ₄₂ protofibrils using computer simulations

Kaur,

Mankoo,

Kaur

et al. 2024

Phys. Chem. Chem. Phys.

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Introduction and Technical Survey: Protein Aggregation and Fibrillogenesis

Harris

Milton

2012

Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease

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In this chapter we provided the overall background to the subject of protein aggregation and fibrillogenesis in amyloidogenesis, with introduction and brief discussion of the various topics that are included with the coming chapters. The division of the book into basic science and clinical science sections enables correlation of the topics to be made. The many proteins and peptides that have currently been found to undergo fibrillogenesis are tabulated. A broad technical survey is made, to indicate the vast array of techniques currently available to study aspects of protein oligomerization, aggregation and fibrillogenesis. These are split into three groups and tabulated, as the microscopical techniques, the analytical and biophysical methods, and the biochemical and cellular techniques. A few techniques are discussed, but in most cases only a link to relevant recent literature is provided.

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AFM and fluorescence spectrascopy investigation for disaggregation of existing Aβ fibrils by baicalein

Cited by 7 publications

References 11 publications

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

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

Insights into the baicalein-induced destabilization of LS-shaped Aβ₄₂ protofibrils using computer simulations

Introduction and Technical Survey: Protein Aggregation and Fibrillogenesis

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AFM and fluorescence spectrascopy investigation for disaggregation of existing Aβ fibrils by baicalein

Cited by 7 publications

References 11 publications

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

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

Insights into the baicalein-induced destabilization of LS-shaped Aβ42 protofibrils using computer simulations

Introduction and Technical Survey: Protein Aggregation and Fibrillogenesis

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Insights into the baicalein-induced destabilization of LS-shaped Aβ₄₂ protofibrils using computer simulations