What peer‑reviewed papers from Brain Chemistry Labs list molecular targets or drug candidates for tangle diseases?
Executive summary
A review of the reporting provided finds no clear peer‑reviewed research papers published by “Brain Chemistry Labs” that explicitly list molecular targets or named drug candidates for tau “tangle” diseases; the Institute’s website promotes the environmental neurotoxin BMAA and L‑serine as an intervention hypothesis and references some peer‑reviewed work but does not itself present a traceable, peer‑reviewed target/drug paper in the material supplied [1] [2]. Independent, peer‑reviewed literature cited in the collection identifies several molecular targets and candidate strategies for tauopathy/tangle diseases — for example, a six‑amino‑acid flexible region in tau as a small‑molecule target (MIT) and kinases such as GSK‑3 and CDK5 implicated in tau phosphorylation [3] [4] [5].
1. What the user’s question actually asks and what the sources allow
The user is asking for peer‑reviewed papers authored by Brain Chemistry Labs that list molecular targets or drug candidates for tangle diseases; the available material consists of Brain Chemistry Labs’ website pages and a set of independent peer‑reviewed articles and reviews, so the search is constrained to whether the Institute’s own publications in the provided set qualify as peer‑reviewed, and what targets are described elsewhere in the supplied literature [1] [2] [6].
2. What Brain Chemistry Labs actually publishes in the provided reporting
Brain Chemistry Labs (Institute for EthnoMedicine) promotes the hypothesis that the cyanobacterial toxin BMAA misincorporates for L‑serine, causing protein misfolding and tangles, and asserts that raising L‑serine can prevent BMAA misincorporation — claims presented on its website and in blog material rather than in an identifiable peer‑reviewed paper provided here [1] [2]. The site also advertises a hair test for BMAA as a putative biomarker and cites collaborations and diagnostic sample handling [1] [2], but the supplied pages do not contain a standalone, traceable peer‑reviewed article from Brain Chemistry Labs that enumerates molecular targets or specific drug candidates for tauopathies [1] [2].
3. Peer‑reviewed work in the supplied set that does list molecular targets or candidate approaches
Independent peer‑reviewed pieces in the supplied reporting do list molecular targets and candidate strategies: MIT chemists identified a six‑amino‑acid flexible sequence in the R2 repeat of tau that may be an accessible target to inhibit tau fibril formation (Science Advances/Nature Communications reporting summarized by MIT) [3] [4] [7]. Reviews and topic overviews cite kinases involved in tau phosphorylation — especially glycogen synthase kinase‑3 (GSK‑3) and cyclin‑dependent kinase‑5 (CDK5) — as potential intervention points to reduce tangle formation [5]. Transcriptomic profiling of NFT‑bearing neurons highlights molecular signatures associated with tangle susceptibility and suggests cellular pathways that could be targeted, though it focuses on vulnerability signatures rather than naming a single drug candidate (Otero‑Garcia et al., Neuron) [6] [8].
4. How Brain Chemistry Labs’ claims fit with peer‑reviewed targets and where gaps remain
The Institute’s BMAA→L‑serine narrative implies a preventive pharmacologic concept — supplement L‑serine to block misincorporation — but the material supplied stops short of a peer‑reviewed, mechanistic drug‑discovery paper from Brain Chemistry Labs that lists validated molecular targets or tested drug candidates for tau pathology [1]. By contrast, the peer‑reviewed literature in the set identifies biochemical mechanisms (tau truncation and conformational flexibility, hyperphosphorylation by kinases) and cell‑type molecular signatures that are nearer to canonical drug targets [3] [4] [5] [6].
5. Bottom line and recommended next steps for a reader following the trail
Based on the supplied reporting, there are no clearly traceable, peer‑reviewed Brain Chemistry Labs papers that formally list molecular targets or named drug candidates for tangle diseases; instead, the Institute’s public materials promote toxin‑driven hypotheses and diagnostics [1] [2]. For bona fide, peer‑reviewed molecular targets and drug approaches consult the independent literature summarized here — the MIT structural work pointing to a six‑amino‑acid flexible region and reviews naming kinases (GSK‑3, CDK5) and transcriptomic studies of NFT‑bearing neurons offer concrete starting points [3] [4] [5] [6]. If confirmation of any Brain Chemistry Labs peer‑reviewed paper is required, primary literature searches (journal databases, PubMed) or direct citation links from the Institute to full articles would be necessary because the provided pages do not supply those peer‑review citations [1] [2].