DeCure's autonomous Rare AI scientist is researching a drug-repurposing hypothesis for amyloidosis — screening already-approved drugs against its 43-gene Open Targets disease module to publish open-access research. Research is fast; the path to publication is funded in milestone stages.
Disease moduleAmyloidosis maps to a 43-gene Open Targets module — the target space DeCure's AI scientist screens approved drugs against.
DeCure.ai methodSignature reversal (LINCS) plus network proximity (STRING) rank already-approved drugs likely to perturb this module — the same engine that produces DeCure.ai's repurposing hypotheses.
Repurposing thesisScreening approved medicines against this disease module, then publishing the evidence for the strongest candidate. Known pharmacology and human exposure data make the first question sharper — they do not establish safety or efficacy in a new indication.
Research record
01
ResearchComing soon
Candidate research + dossier — target rationale, drug-repurposing thesis and evidence pack.proof: Published dossier + on-chain hash
02
ValidationComing soon
In-vitro biological validation at a contract research org (CRO).proof: CRO contract + in-vitro report
03
Peer review & paperComing soon
Peer-reviewed paper published open-access (preprint + journal).proof: DOI + open-access link + on-chain hash
Current lead
approvedDiclofenacCyclooxygenase inhibitor
Structures already discussed alongside amyloidosis in the retrieved literature, rendered from public PubChem SMILES. Which drugs appear here reflects the evidence found, not a ranked prediction.
Molecular view
CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN — Diclofenac has a real, experimentally solved structure in complex with this target (PDB 1DVX, 2.0 Å). This is the drug's own deposited structure, not a prediction, and confirms it is a structurally characterised molecule rather than an untested guess.
Loading structure…
helix sheet difdrag to rotate · scroll to zoom
RCSB Protein Data Bank · entry 1DVX · 2.0 Å · ligand Diclofenac (DIF). Experimental structure, not a prediction.
What the evidence adds up to
A 2015 survey of 533 patients, family members, and caregivers found that for 37.1% of respondents the diagnosis of amyloidosis took a year or more after first symptoms. Patients saw one physician (7.6%), two (23.5%), three (20.3%), four (16.8%), or five or more (31.8%) before diagnosis. Haematologists or oncologists made the correct diagnosis most often (34.1%). Treatments included chemotherapy (63.1%) and stem cell transplantation (38.9%), and 54.1% of respondents found treatment difficult to tolerate. Nearly half (46.1%) believed enrolling in a clinical trial would improve their care, but many felt uninformed about trials.
In a 2014 mouse model of AA amyloidosis, prophylactic treatment with diclofenac alone showed no positive effect on amyloid deposition. Combined prophylactic diclofenac and prednisolone significantly reduced amyloid deposits in spleen, kidneys, and liver (P < 0.02–0.001). Sulfasalazine alone was more successful prophylactically, with statistically significant decreases in all investigated organs (P < 0.04–0.001) and the strongest suppression in kidneys and liver (P < 0.004–0.001). In therapeutic treatment, combined diclofenac and prednisolone showed the most inhibition, with the highest suppression (86.7%; P < 0.001) in the liver. Diclofenac alone reduced amyloid only in the liver (P < 0.03), and sulfasalazine alone only in the spleen (P < 0.03). None of the drugs completely inhibited disease in this model.
A 2023 case report describes the first known coexistence of tracheobronchial amyloidosis and acute myeloid leukaemia. A 2016 report notes that amyloidosis is a rare, progressive, often fatal disease with nonspecific early serologic and imaging findings, making diagnosis difficult. A 2025 review states that amyloid deposits disrupt normal organ function and can lead to organ failure, and that early diagnosis and treatment are crucial.
What is still missing: no clinical trial has tested sulfasalazine, diclofenac, or prednisolone for amyloidosis in patients. The mouse data are prophylactic and therapeutic but not replicated in humans. Patient awareness of trials remains low, and no well-tolerated therapy with clear treatment benefit has been identified for AL amyloidosis. Stratification by amyloid type and organ involvement is not addressed in these studies.
Evidence
Retrieved by DeepSearch across 234,678,978 indexed works and resolved on OpenAlex — ranked by citations, including the results that did not work.
Advances in Therapy · 2015 · 270 citations · open access
Light Chain Amyloidosis: Patient Experience Survey from the Amyloidosis Research Consortium
AbstractINTRODUCTION: Information detailing the experience of patients with light chain (AL) amyloidosis is lacking. The primary aim of this study was to gather data on the patient experience to understand the challenges in diagnosis and to gain insight into barriers to accessing appropriate care. METHODS: Patients with amyloidosis, family members, and caregivers were invited to participate in an online 16-question survey (available from January 29 to February 5, 2015). Participants with AL amyloidosis were sent an eight-question follow-up survey. RESULTS: The initial survey was completed by 533 participants (follow-up survey completed by 201 participants). AL amyloidosis was the most common diagnosis. For 37.1% of respondents, the diagnosis of amyloidosis was not established until ≥ 1 year after the onset of initial symptoms. Diagnosis was received after visits to 1, 2, 3, 4, or ≥ 5 physicians by 7.6%, 23.5%, 20.3%, 16.8%, and 31.8% of respondents, respectively. Correct diagnosis was most often made by hematologists/oncologists (34.1%). Treatments included chemotherapy (63.1%) and stem cell transplantation (38.9%) and were difficult to tolerate for 54.1% of respondents. A significant number of respondents felt uninformed about clinical trials. Nevertheless, approximately half (46.1%) believed that enrolling in a trial would enhance their care. CONCLUSIONS: Establishing a diagnosis of amyloidosis is difficult. Current treatments are difficult to tolerate and do not substantially improve quality of life for most patients. There is an urgent need for well-tolerated therapies with clear treatment benefit. Patient awareness of clinical trials can be improved, especially given that respondents indicated high willingness to participate.
Ajakirjad. Journals by UT · 2014 · 1 citations · open access
Effects of Antirheumatic Drugs on the Development of Experimental AA Amyloidosis in C57BL/6 Mice
AbstractBecause there is no known specific effective therapy for secondary amyloidosis at the present time, the aim of this study was to determine whether antirheumatic drugs inhibit the development of experimental AA amyloidosis, induced in a C57BL/6 mice by injections of casein and fibrin. Monotherapy with sulfasalazine (SSL) and diclofenac (D) and combined treatment with diclofenac and prednisolone (D/P) by using prophylactic and therapeutic treatment protocols were investigated. The drugs were administered through intragastric gavage 5 times a week for 5 or 6 weeks in the following doses: D - 1 mg/kg, P - 10 mg/kg, and SSL - 100 mg/kg. Histopathological examination of splenic, kidney and hepatic tissues of mice was performed. The amount of amyloid was assessed semi-quantitatively by polarizing microscopy after Congo Red staining. Our study indicated that no positive effect from prophylactic treatment with D could be seen on amyloid deposition in investigated organs. Prophylactic combined treatment with D/P resulted in significant improvement of disease symptoms and markedly reduced amyloid deposits in the spleen, kidneys, and liver (P < 0.02-0.001). SSL therapy alone has been more successful in the prophylactic treatment of experimental amyloidosis: the decrease of amyloid deposits was statistically significant in all investigated organs (P < 0.04 – 0.001) and the most suppression of amyloid formation in the kidneys and liver was observed (P < 0.004-0.001). In therapeutic treatment of experimental amyloidosis, combined treatment with D/P showed the most inhibition of amyloid formation in the internal organs (P < 0.006 – 0.001). The highest suppression (by 86.7%; P < 0.001) of amyloid deposits was observed in the liver. Treatment of mice with D alone produced a significant reduction in amyloid deposition only in the liver (P < 0.03) and with SSL – only in the spleen (P < 0.03). These findings suggest that D/P and SSL at relevant doses suppress amyloidogenesis and this suppression is possibly related to the anti-inflammatory effect of antirheumatic drugs. Although these drugs cannot completely inhibit the disease in this model, a possibility remains that they may be clinically useful in rheumatic diseases associated with the formation of amyloidogenic derivatives.
A case of tracheobronchial amyloidosis presentingwith acute myeloid leukemia
AbstractLocalized tracheobronchial amyloidosis (TBA) is a rare form of pulmonary amyloidosis that is characterized by amyloidosis accumulation in the trachea and main bronchus submucosa.TBA is usually localized in the lung and is not associated with systemic amyloidosis.Although patients may be asymptomatic at first, they may develop dyspnea, recurrent cough, and hemoptysis attacks as the lesions narrow the tracheobronchial tree.Histochemical examination of biopsies taken with flexible bronchoscopy after thorax CT findings is usually used to make the diagnosis.There has never been a case reported in which TBA and acute myeloid leukemia (AML) coexisted.We report the first case of TBA in a patient diagnosed with AML.
Zenodo (CERN European Organization for Nuclear Research) · 2025 · 0 citations · open access
FEATURES OF THE PATHOLOGICAL AND ANATOMICAL MANIFESTATION OF AMYLOIDOSIS
AbstractAmyloidosis is a group of diseases characterized by the abnormal extracellular deposition of amyloid proteins in various tissues and organs. These deposits disrupt normal function and can lead to organ failure. Amyloidosis may be systemic or localized, with several biochemical types. Early diagnosis and treatment are crucial to improving outcomes. Key words: abnormal, proteins, organ, eosinophilic, pathological anatomy, myloidosis, diagnosis.
Oxford University Press eBooks · 2016 · 0 citations
A Rare Cause of Liver Failure
AbstractAbstract Amyloidosis is a rare, progressive, and often fatal disease that is notably difficult to diagnose because of nonspecific serologic and imaging studies during the initial stages. However, early recognition and diagnosis are crucial for treatment, which may limit and reverse organ dysfunction. The exact incidence of amyloidosis is unknown.
Disease module: DeepOracle (Open Targets). Structures: RDKit from PubChem SMILES. Literature: retrieved by DeepSearch across 234,678,978 indexed works (targeted per-candidate search), resolved on OpenAlex.
DeCure is a research and publication project, not medical advice and not a treatment. "DeCure for X" describes a research goal, not a claim that a cure exists. Backing a cure is a contribution to fund the research — it is not an investment, and confers no yield, royalty, equity or IP ownership. Papers are published open-access by the DeCure.ai DAO.
