In vitro antiamyloidogenic properties of 1,4-naphthoquinones

Bermejo-Bescós, Paloma; Martín‐Aragón, Sagrario; Jiménez-Aliaga, Karim; Giménez, Alfonso Ortega; Molina, Marı́a Teresa; Buxaderas, Eduardo; Orellana, Guillermo; Csákÿ, Aurelio G.

doi:10.1016/j.bbrc.2010.08.038

Cited by 44 publications

(37 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…at a dose of 50 mg/kg protected rodents against experimental stroke with an increase in the enzymatic activities of catalase (CAT), superoxide dismutase (SOD), and glutathione peroxidase (GPx) and a decrease in ROS. 155 Naphthoquinones not only are neurotrophic but also inhibit the enzymatic activity of enzymes involved in the pathophysiology of neurodegenerative diseases. 128 In the same experiment, 5E5 (CS 3.124) at a dose of 1 μM induced TrkA, Akt, ERK1/2, FRS2/SNT, and neurite outgrowth in PC12 cells exposed to NGF.…”

Section: Phytopharmacologymentioning

confidence: 99%

Phenolics

Wiart

2014

Lead Compounds From Medicinal Plants for the Treatment of Neurodegenerative Diseases

View full text Add to dashboard Cite

Section: Phytopharmacologymentioning

confidence: 99%

Phenolics

Wiart

2014

Lead Compounds From Medicinal Plants for the Treatment of Neurodegenerative Diseases

View full text Add to dashboard Cite

“…Similarly, 9,10-anthraquinone strongly inhibits the aggregation of β-amyloid protein28. In addition, several derivatives of 1,4-naphthoquinone have been explored as drug candidates for amyloidosis diseases29. These evidences all implicate quinones as a class of compounds with inhibitory effect on protein misfolding and aggregation.…”

mentioning

confidence: 99%

Effects of several quinones on insulin aggregation

Gong

Peng

et al. 2014

Sci Rep

131

View full text Add to dashboard Cite

Protein misfolding and aggregation are associated with more than twenty diseases, such as neurodegenerative diseases and metabolic diseases. The amyloid oligomers and fibrils may induce cell membrane disruption and lead to cell apoptosis. A great number of studies have focused on discovery of amyloid inhibitors which may prevent or treat amyloidosis diseases. Polyphenols have been extensively studied as a class of amyloid inhibitors, with several polyphenols under clinical trials as anti-neurodegenerative drugs. As oxidative intermediates of natural polyphenols, quinones widely exist in medicinal plants or food. In this study, we used insulin as an amyloid model to test the anti-amyloid effects of four simple quinones and four natural anthraquinone derivatives from rhubarb, a traditional herbal medicine used for treating Alzheimer's disease. Our results demonstrated that all eight quinones show inhibitory effects to different extent on insulin oligomerization, especially for 1,4-benzoquinone and 1,4-naphthoquinone. Significantly attenuated oligomerization, reduced amount of amyloid fibrils and reduced hemolysis levels were found after quinones treatments, indicating quinones may inhibit insulin from forming toxic oligomeric species. The results suggest a potential action of native anthraquinone derivatives in preventing protein misfolding diseases, the quinone skeleton may thus be further explored for designing effective anti-amyloidosis compounds.

show abstract

“…In spite of this, tacrine is being and has been used as a template to design new non‐hepatotoxic analogues for AD . On the other hand, quinones are very well known A β ‐aggregation inhibitors,, and consequently, their use as a selected pharmacophoric motif to be incorporated in our target compounds, instead of the benzene ring A in tacrine (Figure ), would be very well justified. However, it is true that until now no agent based on the so‐called A β hypothesis has been clinically approved …”

Section: Introductionmentioning

confidence: 99%

Synthesis, Biological Assessment and Molecular Modeling of Racemic QuinoPyranoTacrines for Alzheimer's Disease Therapy

et al. 2018

View full text Add to dashboard Cite

In this report we describe the synthesis, biological evaluation and molecular modeling of new tacrine analogues such as QuinoPyranTacrines (QPTs), designed by juxtaposition of 1,4‐naphthoquinone and tacrine. From these results we have identified QPT16 as a permeable, selective human acetylcholinesterase inhibitor [IC50= 1.1 ± 0.15 μM], 3.5‐fold less‐hepatotoxic than tacrine at 1000 μM concentration, and consequently, a potential new hit‐compound for further investigation targeted to find a new agent for AD therapy.

show abstract

In vitro antiamyloidogenic properties of 1,4-naphthoquinones

Cited by 44 publications

References 36 publications

Phenolics

Phenolics

Effects of several quinones on insulin aggregation

Synthesis, Biological Assessment and Molecular Modeling of Racemic QuinoPyranoTacrines for Alzheimer's Disease Therapy

Contact Info

Product

Resources

About