Resveratrol inhibits beta-amyloid oligomeric cytotoxicity but does not prevent oligomer formation

Feng, Ying; Wang, Xiaoping; Yang, Sherry; Wang, Yujiong; Zhang, Xi; Du, Xueting; Sun, Xiaoxia; Zhao, Min; Huang, Lei; Liu, Rui‐tian

doi:10.1016/j.neuro.2009.08.013

Cited by 264 publications

(219 citation statements)

References 70 publications

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“…In addition, this observation suggested an effect of the reduced amount of Aβ 40 fibrils in solution that could have acted as seeds to catalyze the Aβ 40 aggregation. As the results from this study were in agreement with previous investigations of resveratrol as Aβ -targeting agents for Alzheimer's disease, [57][58][59] EIS proved to be a useful tool to assist in the elucidation of Aβ aggregation in the presence of small molecule modulators. 40 aggregation with Resveratrol.-Aβ 40 aggregation in the presence and absence of resveratrol was also observed using Thioflavin T (ThT) fluorescence ( Figure 4B).…”

Section: Resultssupporting

confidence: 89%

Electrochemical Detection of Amyloid-Beta Aggregation in the Presence of Resveratrol

Hung

Cheng

et al. 2013

J. Electrochem. Soc.

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The aggregation of amyloid-β (Aβ) is an important pathologic feature of Alzheimer's disease (AD) that leads to the formation of neuronal plaques. A rapidly growing number of polyphenols have been intensively investigated for AD treatment. In this report, the interaction of a polyphenolic compound, resveratrol, with Aβ was studied using electrochemical impedance spectroscopy (EIS). The growth of Aβ fibrils was facilitated with the incubation of oligomer-modified electrodes with free Aβ in solution. Resveratrol significantly slowed down the formation of Aβ aggregates, which was monitored by following the changes in the charge transfer resistance (R ct ) values. The moderating effect of resveratrol on Aβ aggregation was also confirmed with Thioflavin T (ThT) fluorescence assay and transmission electron microscopy (TEM) imaging. Results obtained from EIS correlated well with the ThT fluorescence assay and suggested that EIS was a promising method for the analysis of Aβ aggregation in the presence of novel Aβ-targeting compounds toward AD therapy. Various factors contribute to the deterioration of health in the aging population. Of those, dementia is a prominent worldwide issue that is currently under intense investigation in an effort to discover novel therapeutic agents to slow the progression of this disease. Alzheimer's disease (AD) has been found to be the most common cause of dementia, in which a multitude of regulatory pathways are affected. As the disease progresses, physical manifestations include reduced mobility, changes in behavior and a decline in cognitive function.

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Section: Resultssupporting

confidence: 89%

Electrochemical Detection of Amyloid-Beta Aggregation in the Presence of Resveratrol

Hung

Cheng

et al. 2013

J. Electrochem. Soc.

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“…Moreover, SIRT1 overexpression reduces Ab pathology in APP-expressing neuronal cultures by delaying Ab synthesis (Marambaud et al, 2005;Tang and Chua, 2008). Feng et al demonstrated that resveratrol disrupts Ab hydrogen binding, preventing fibril formation by destabilizing preformed fibrils without affecting oligomerization (Feng et al, 2009). Furthermore, studies have shown that the protective effects of resveratrol on b-amyloid-induced toxicity are related to activation of PKC or AMPK (Han et al, 2004;Karuppagounder et al, 2009).…”

Section: Resveratrol and Sirt1mentioning

confidence: 99%

Antioxidant effects of resveratrol in cardiovascular, cerebral and metabolic diseases

Carrizzo

Forte

Damato

et al. 2013

Food and Chemical Toxicology

174

105

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a b s t r a c tResveratrol-a natural polyphenolic compound-was first discovered in the 1940s. Although initially used for cancer therapy, it has shown beneficial effects against most cardiovascular and cerebrovascular diseases. A large part of these effects are related to its antioxidant properties. Here we review: (a) the sources, the metabolism, and the bioavailability of resveratrol; (b) the ability of resveratrol to modulate redox signalling and to interact with multiple molecular targets of diverse intracellular pathways; (c) its protective effects against oxidative damage in cardio-cerebro-vascular districts and metabolic disorders such as diabetes; and (d) the evidence for its efficacy and toxicity in humans. The overall aim of this review is to discuss the frontiers in the field of resveratrol's mechanisms, bioactivity, biology, and healthrelated use.

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“…Red wine represents a rich source of polyphenols such as flavonoids (flavanol *Address correspondence to this author at the Department of Biochemistry and Molecular Biology, Faculty of Science and Informatics, University of Szeged, H-6726 Szeged, Középfasor 52, Hungary; Tel: +36-62-544543; Fax: +36-62-544887; E-mail: kotorman@expbio.bio.u-szeged.hu monomers, condensed tannins, flavonols, anthocyanins) as well as non-flavonoids (hydroxycinnamates, benzoic acids, hydrolyzable tannins and stilbenes (resveratrol)) [8]. Resveratrol, a polyphenolic red wine constituent, inhibits Aβ42 fibril formation and islet amyloid polypeptide aggregation in a dose-dependent manner [9][10]. The inhibitory effect of flavone derivatives is dependent on the number and position of hydroxyl groups around the flavone backbone [11].…”

Section: Introductionmentioning

confidence: 99%

Inhibition of Amyloid-like Fibril Formation of Trypsin by Red Wines

Kotormán

Kasi

Halász

et al. 2017

PPL

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Abstract:The aim of the present study was to examine the potential role and applicability of dietary supplements in reducing the risk of development of amyloid diseases associated with the gastrointestinal tract, such as type II diabetes. Trypsin, a well-known serine protease was used as a model protein in our experiments. The effect of various red wines on the formation of amyloid-like fibrils of trypsin was studied in vitro, in aqueous ethanol, at pH 7.0. Turbidity measurements, aggregation kinetics experiments, Congo red binding assays and electronic circular dichroism spectroscopic measurements were used to follow the aggregation process in the presence or absence of various red wines. The results suggest that red wines effectively inhibit the formation of amyloid-like fibrils of trypsin and the inhibitory effect is dose-dependent. The extent of inhibition was found to be proportional to the total concentration of phenolic compounds.

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Resveratrol inhibits beta-amyloid oligomeric cytotoxicity but does not prevent oligomer formation

Cited by 264 publications

References 70 publications

Electrochemical Detection of Amyloid-Beta Aggregation in the Presence of Resveratrol

Electrochemical Detection of Amyloid-Beta Aggregation in the Presence of Resveratrol

Antioxidant effects of resveratrol in cardiovascular, cerebral and metabolic diseases

Inhibition of Amyloid-like Fibril Formation of Trypsin by Red Wines

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