ArticleProtein science : a publication of the Protein Society2013
Characterizing antiprion compounds based on their binding properties to prion proteins: implications as medical chaperones.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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27 citing papers in PubMed, 62 citations in OpenAlex.
- Inhibition of amyloid formation of prion fragment (106-128) by polyphenolic compounds.Biochimica et biophysica acta. General subjects · 2025Article
- Therapeutic Trajectories in Human Prion Diseases.Sub-cellular biochemistry · 2025Review
- Altered properties of amyloidogenic prion protein in genetic Creutzfeldt-Jakob disease with PRNP V180I mutation in response to pentosan polysulfate.Brain pathology (Zurich, Switzerland) · 2023Article
- Prion therapeutics: Lessons from the past.Prion · 2022Review
- Article
- Ligands binding to the prion protein induce its proteolytic release with therapeutic potential in neurodegenerative proteinopathies.Science advances · 2021Article
- Volatile Anesthetic Sevoflurane Precursor 1,1,1,3,3,3-Hexafluoro-2-Propanol (HFIP) Exerts an Anti-Prion Activity in Prion-Infected Culture Cells.Neurochemical research · 2021Article
- Unfolded and intermediate states of PrP play a key role in the mechanism of action of an antiprion chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Green Tea Polyphenol Epigallocatechin-Gallate in Amyloid Aggregation and Neurodegenerative Diseases.Frontiers in neuroscience · 2021Review
- Article
- BMD42-2910, a Novel Benzoxazole Derivative, Shows a Potent Anti-prion Activity and Prolongs the Mean Survival in an Animal Model of Prion Disease.Experimental neurobiology · 2020Article
- Identifying Anti-prion Chemical Compounds Using a Newly Established Yeast High-Throughput Screening System.Cell chemical biology · 2019Article
- Direct interaction of DNMT inhibitors to PrPActa pharmaceutica Sinica. B · 2019Article
- Article
- Application of the fragment molecular orbital method to discover novel natural products for prion disease.Scientific reports · 2018Article
- Pharmacological Agents Targeting the Cellular Prion Protein.Pathogens (Basel, Switzerland) · 2018Review
- Insights from Therapeutic Studies for PrP Prion Disease.Cold Spring Harbor perspectives in medicine · 2017Review
- Effects of ligand binding on the stability of aldo-keto reductases: Implications for stabilizer or destabilizer chaperones.Protein science : a publication of the Protein Society · 2016Article
- Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein.Nature communications · 2016Article
- A cationic tetrapyrrole inhibits toxic activities of the cellular prion protein.Scientific reports · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A variety of antiprion compounds have been reported that are effective in ex vivo and in vivo treatment experiments. However, the molecular mechanisms for most of these compounds remain unknown. Here we classified antiprion mechanisms into four categories: I, specific conformational stabilization; II, nonspecific stabilization; III, aggregation; and IV, interaction with molecules other than PrP(C). To characterize antiprion compounds based on this classification, we determined their binding affinities to PrP(C) using surface plasmon resonance and their binding sites on PrP(C) using NMR spectroscopy. GN8 and GJP49 bound specifically to the hot spot in PrP(C), and acted as "medical chaperones" to stabilize the native conformation. Thus, mechanisms I was predominant. In contrast, quinacrine and epigallocathechin bound to PrP(C) rather nonspecifically; these may stabilize the PrP(C) conformation nonspecifically including the interference with the intermolecular interaction following mechanism II. Congo red and pentosan polysulfate bound to PrP(C) and caused aggregation and precipitation of PrP(C), thus reducing the effective concentration of prion protein. Thus, mechanism III was appropriate. Finally, CP-60, an edarabone derivative, did not bind to PrP(C). Thus these were classified into mechanism IV. However, their antiprion activities were not confirmed in the GT + FK system, whose details remain to be elucidated. This proposed antiprion mechanisms of diverse antiprion compounds could help to elucidate their antiprion activities and facilitate effective antiprion drug discovery.
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