Quercetin binding accelerates prion fibrillation into proteinase sensitive and loosely structured amyloids

Yu, Kun-Hua; Jheng, Cheng-Ping; Lee, Cheng-I

doi:10.1016/j.biopha.2022.113177

Cited by 7 publications

(6 citation statements)

References 46 publications

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“…Oxidative stress has been identified as a hallmark of neurodegeneration [ 32 , [129] , [130] , [131] ]. In accordance with other anti-oxidant compounds exhibiting anti-prion activity [ 72 , 124 , 126 , 128 , 132 , 133 ], Oenin and Myrtillin successfully decreased the levels of ROS in prion-infected cells. While Oenin didn't affect Nrf2 expression levels, it managed to activate the Keap1-Nrf2 pathway (albeit less effectively compared to Myrtillin).…”

Section: Discussionsupporting

confidence: 74%

“…Indeed, other flavonoids are capable of directly binding to PrP C . For example, Quercetin, interaction with PrP Sc fibrils renders them vulnerable to protein degradation, leading to de-aggregation [ 123 , 124 ]. Moreover, Apigenin and Nepetin managed to inhibit the fibrillation of the PrP 106-126 peptide and also depolymerize the already formed fibrils [ 125 ].…”

Section: Discussionmentioning

confidence: 99%

“…It is also worth noting that, Oenin and Myrtillin might exert their anti-prion action with a combination of different mechanisms. Quercetin can simultaneously bind to the C-terminal region of murine prion protein and also act as an anti-oxidant [ 124 , 126 ]. A similar observation was made with Curcumin, which can bind to PrP Sc fibrils, as well as intermediate aggregates of the PrP C –PrP Sc conversion, while also exerting anti-oxidant action [ 127 , 128 ].…”

Section: Discussionmentioning

confidence: 99%

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Αnti-prion effects of anthocyanins

Christoudia,

Bekas,

Kanata

et al. 2024

Redox Biology

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Section: Discussionsupporting

confidence: 74%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Αnti-prion effects of anthocyanins

Christoudia,

Bekas,

Kanata

et al. 2024

Redox Biology

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“…The transition of Lys194 and Glu196 from intramolecular to intermolecular interaction is important to the PrP C -PrP Sc conversion. In our MD simulation, quercetin accelerates the low toxic and PK-sensitive fibril formation by weakening the fibril structure and interacting with PrP protein at Glu196 ( Yu et al, 2022 ). The same binding residue consists of the MD result from the quercetin-fPrP 170–229 complex in this work.…”

Section: Discussionmentioning

confidence: 97%

“…Recently, we found that quercetin disaggregates mature prion fibrils, accelerates fibril clearance with PK, and reduces ROS levels in Neuro-2a cells ( Yu and Lee, 2020 ). In addition, quercetin binding accelerates the formation of PK-sensitive and structure-less fibrils ( Yu et al, 2022 ).…”

Section: Introductionmentioning

confidence: 99%

Combination of structure-based virtual screening, molecular docking and molecular dynamics approaches for the discovery of anti-prion fibril flavonoids

Jheng

Lee

2023

Front. Mol. Biosci.

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Prion diseases are a group of rare neurodegenerative diseases caused by the structural conversion of cellular prion into Scrapie prion resulting aggregated fibrils. Therapy of prion diseases has been developed for several decades, especially drug designs based on the structure of prion monomers. Unfortunately, none of the designed anti-prion drugs function well clinically. To fight against prion fibrils, a drug design based on the precise structure of mammalian prion fibrils is highly required. Fortunately, based on the advantage of newly advanced cryo-electron microscopy (cryo-EM) in the deconvolution of large complexes, three prion fibril structures were resolved in the last 2 years. Based on the cryo-EM solved prion fibril structures, we are able to find some molecules fighting against prion fibrils. Quercetin, one flavonoid molecule in the polyphenol group, has been found to disaggregate the prion fibrils in vitro. In this study, we performed the molecular docking and molecular dynamics simulation on quercetin-like molecules possessing pharmacological properties to evaluate the anti-prion ability of tested molecules. As a result, four quercetin-like molecules interact with prion fibril and decrease the β-strand content by converting some β-strands into loop and helical structures to disintegrate the existing fibril structure. The results of this study are significant in the treatment of prion diseases, and the approaches used in this study are applicable to other amyloid diseases.

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Biopolymer Nanovehicles for Oral Delivery of Natural Anticancer Agents

Falsafi

Wang

Ashaolu

et al. 2022

Adv Funct Materials

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Cancer is the second leading cause of death throughout the world. Nature‐inspired anticancer agents (NAAs) that are a gift of nature to humanity have been extensively utilized in the alleviation/prevention of the disease due to their numerous pharmacological activities. While the oral route is an ideal and common way of drug administration, the application of NAAs through the oral pathway has been extremely limited owing to their inherent features, e.g., poor solubility, gastrointestinal (GI) instability, and low bioavailability. With the development of nano‐driven encapsulation strategies, polymeric vehicles, especially those with natural origins, have demonstrated a potent platform, which can professionally shield versatile NAAs against GI barricades and safely deliver them to the site of action. In this review, the predicament of orally delivering NAAs and the encapsulation strategy solutions based on biopolymer matrices are summarized. Proof‐of‐concept in vitro/in vivo results are also discussed for oral delivery of these agents by various biopolymer vehicles, which can be found so far from the literature. Last but not the least, the challenges and new opportunities in the field are highlighted.

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Quercetin binding accelerates prion fibrillation into proteinase sensitive and loosely structured amyloids

Cited by 7 publications

References 46 publications

Αnti-prion effects of anthocyanins

Αnti-prion effects of anthocyanins

Combination of structure-based virtual screening, molecular docking and molecular dynamics approaches for the discovery of anti-prion fibril flavonoids

Biopolymer Nanovehicles for Oral Delivery of Natural Anticancer Agents

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