ArticleScientific reports2020
CMT-3 targets different α-synuclein aggregates mitigating their toxic and inflammogenic effects.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Smart Drug-Delivery Approaches for Enhanced Management of Comorbid Conditions in Alzheimer's Disease.Life (Basel, Switzerland) · 2026Review
- DDOX expands the repertoire of tetracyclines for Parkinson's disease by preventing the cellular uptake and intracellular impact of α-synuclein preformed fibrils.Scientific reports · 2025Article
- Protein Coaggregation in Caribbean Atypical Parkinsonism: The Contribution of Annonacin.Neuropathology and applied neurobiology · 2025Article
- A Novel Small Molecule Enhances Stable Dopamine Delivery to the Brain in Models of Parkinson's Disease.International journal of molecular sciences · 2025Article
- Review
- Repositioning of drugs for Parkinson's disease and pharmaceutical nanotechnology tools for their optimization.Journal of nanobiotechnology · 2022Review
- Article
- Challenges of repurposing tetracyclines for the treatment of Alzheimer's and Parkinson's disease.Journal of neural transmission (Vienna, Austria : 1996) · 2022Review
- Tetracycline ameliorates silica-induced pulmonary inflammation and fibrosis via inhibition of caspase-1.Respiratory research · 2022Article
- Article
- Targeting Microglial α-Synuclein/TLRs/NF-kappaB/NLRP3 Inflammasome Axis in Parkinson's Disease.Frontiers in immunology · 2021Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Parkinson's disease (PD) is a neurodegenerative disorder for which only symptomatic treatments are available. Repurposing drugs that target α-synuclein aggregation, considered one of the main drivers of PD progression, could accelerate the development of disease-modifying therapies. In this work, we focused on chemically modified tetracycline 3 (CMT-3), a derivative with reduced antibiotic activity that crosses the blood-brain barrier and is pharmacologically safe. We found that CMT-3 inhibited α-synuclein amyloid aggregation and led to the formation of non-toxic molecular species, unlike minocycline. Furthermore, CMT-3 disassembled preformed α-synuclein amyloid fibrils into smaller fragments that were unable to seed in subsequent aggregation reactions. Most interestingly, disaggregated species were non-toxic and less inflammogenic on brain microglial cells. Finally, we modelled the interactions between CMT-3 and α-synuclein aggregates by molecular simulations. In this way, we propose a mechanism for fibril disassembly. Our results place CMT-3 as a potential disease modifier for PD and possibly other synucleinopathies.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.