Activities of curcumin-related compounds in two cell lines persistently infected with different prion strains

Teruya, Kenta; Iwabuchi, Sara; Watanabe, Yuki; Tsuchida, Rikiya; Watanabe-Matsui, Miki; Konno, Hiroyuki; Doh‐ura, Katsumi

doi:10.1016/j.bbagen.2022.130094

Cited by 4 publications

(4 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Section: Resultsmentioning

confidence: 99%

“…The compounds tested in this screening included astemizole, curcumin, quinacrine dihydrochloride, imatinib, resveratrol, azure A, azure B, azure C, thioflavin, tetracycline, tannic acid, tetradrine, quinacrine mustard, rhodamine and thionine acetate. 30,[56][57][58][59][60][61][62][63][64][65][66][67] Most anti-prion molecules were selected based on their effectiveness against RML prions, as previously reported in a cell-based assay. 21 On the other hand, the six anti-amyloid compounds have been previously tested against misfolded proteins associated with Parkinson's and Alzheimer's diseases (α-synuclein and amyloid-β, respectively).…”

Section: Screening Of Known Anti-prion and Anti-amyloid Molecules Aga...mentioning

confidence: 99%

See 1 more Smart Citation

Adaptation of the protein misfolding cyclic amplification (PMCA) technique for the screening of anti‐prion compounds

Do,

Benavente,

Catumbela

et al. 2024

The FASEB Journal

View full text Add to dashboard Cite

Prion diseases result from the misfolding of the physiological prion protein (PrPC) to a pathogenic conformation (PrPSc). Compelling evidence indicates that prevention and/or reduction of PrPSc replication are promising therapeutic strategies against prion diseases. However, the existence of different PrPSc conformations (or strains) associated with disease represents a major problem when identifying anti‐prion compounds. Efforts to identify strain‐specific anti‐prion molecules are limited by the lack of biologically relevant high‐throughput screening platforms to interrogate compound libraries. Here, we describe adaptations to the protein misfolding cyclic amplification (PMCA) technology (able to faithfully replicate PrPSc strains) that increase its throughput to facilitate the screening of anti‐prion molecules. The optimized PMCA platform includes a reduction in sample and reagents, as well as incubation/sonication cycles required to efficiently replicate and detect rodent‐adapted and cervid PrPSc strains. The visualization of PMCA products was performed via dot blots, a method that contributed to reduced processing times. These technical changes allowed us to evaluate small molecules with previously reported anti‐prion activity. This proof‐of‐principle screening was evaluated for six rodent‐adapted prion strains. Our data show that these compounds targeted either none, all or some PrPSc strains at variable concentrations, demonstrating that this PMCA system is suitable to test compound libraries for putative anti‐prion molecules targeting specific PrPSc strains. Further analyses of a small compound library against deer prions demonstrate the potential of this new PMCA format to identify strain‐specific anti‐prion molecules. The data presented here demonstrate the use of the PMCA technique in the selection of prion strain‐specific anti‐prion compounds.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Screening Of Known Anti-prion and Anti-amyloid Molecules Aga...mentioning

confidence: 99%

Adaptation of the protein misfolding cyclic amplification (PMCA) technique for the screening of anti‐prion compounds

Do,

Benavente,

Catumbela

et al. 2024

The FASEB Journal

View full text Add to dashboard Cite

show abstract

“…In contrast, the proline-catalyzed aldol reaction 46 71), C5-CUR (37), and chalcone (38) and (39), exhibited inhibition of abnormal prion protein propagation in persistently prion-infected cells. 48 Their structureactivity relationships indicate that their hydrogen bonding and hydrophobicities contribute to their biological activities much more than their size.…”

Section: Curcumin Analogues IImentioning

confidence: 99%

“…46) and diaryl γ-dihydropyrone (47) A series of γ-dihydropyrone derivatives (47) was synthesized according to Khera's method. 52 Aldol reaction of acetophenone (40) with ethyl acetate in the presence of NaHMDS afforded the diketone derivative (48), which was treated with NaHMDS and then a variety of benzaldehyde (49) to give the corresponding hydroxy diketone (50) and then dehydration via γ-tetrahydropyrone (51) to give γ-dihydropyrone (52).…”

Section: Diaryl γ-Dihydropyrone Type Analoguesmentioning

confidence: 99%

Design, Synthesis and Evaluation of Catechol-Based Amyloid Beta Aggregation Inhibitors

Konno¹,

Teruya²

2023

HETEROCYCLES

Self Cite

View full text Add to dashboard Cite

The use of small molecules to inhibit amyloid β aggregation is one approach under investigation to prevent the onset of Alzheimer's disease (AD). One such small molecule is curcumin, but its utility is limited by poor water solubility and hence poor bioavailability. In this review, we summarize the findings of structure-activity relationship studies of curcumin and diaryl γ-dihydropyrone, undertaken to improve their inhibitory effect and physical properties. The key findings are: phenolic hydroxy groups can be introduced at the 2 and 3,4-positions of phenol rings, the C7 spacer of curcumin is essential for good anti-amyloid β aggregation activity; and the catechol moiety is important for both anti-aggregation activity and water solubility. The combination of the C5 spacer unit and mono ketone of curcumin analogues is more effective for water solubility with high antiamyloid β aggregation activity. Diaryl γ-dihydropyrone with hydroxy groups on phenol rings as cyclocurcumin mimetics also showed anti-amyloid β aggregation activity and high water solubility. Analogues of berberine, a benzylisoquinoline alkaloid also of interest to treat central nervous system diseases, are also reviewed.Finally, we review efforts to develop fluorescent curcumin analogues for use as diagnostic agents.

show abstract

Curcumin as a natural potential drug candidate against important zoonotic viruses and prions: A narrative review

Azarkar,

Abedi,

Lavasani

et al. 2024

Phytotherapy Research

View full text Add to dashboard Cite

Zoonotic diseases are major public health concerns and undeniable threats to human health. Among Zoonotic diseases, zoonotic viruses and prions are much more difficult to eradicate, as they result in higher infections and mortality rates. Several investigations have shown curcumin, the active ingredient of turmeric, to have wide spectrum properties such as anti‐microbial, anti‐vascular, anti‐inflammatory, anti‐tumor, anti‐neoplastic, anti‐oxidant, and immune system modulator properties. In the present study, we performed a comprehensive review of existing in silico, in vitro, and in vivo evidence on the antiviral (54 important zoonotic viruses) and anti‐prion properties of curcumin and curcuminoids in PubMed, Google Scholar, Science Direct, Scopus, and Web of Science databases. Database searches yielded 13,380 results, out of which 216 studies were eligible according to inclusion criteria. Of 216 studies, 135 (62.5%), 24 (11.1%), and 19 (8.8%) were conducted on the effect of curcumin and curcuminoids against SARS‐CoV‐2, Influenza A virus, and dengue virus, respectively. This review suggests curcumin and curcuminoids as promising therapeutic agents against a wide range of viral zoonoses by targeting different proteins and signaling pathways.

show abstract

Activities of curcumin-related compounds in two cell lines persistently infected with different prion strains

Cited by 4 publications

References 47 publications

Adaptation of the protein misfolding cyclic amplification (PMCA) technique for the screening of anti‐prion compounds

Adaptation of the protein misfolding cyclic amplification (PMCA) technique for the screening of anti‐prion compounds

Design, Synthesis and Evaluation of Catechol-Based Amyloid Beta Aggregation Inhibitors

Curcumin as a natural potential drug candidate against important zoonotic viruses and prions: A narrative review

Contact Info

Product

Resources

About