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fosfosal (fosfosal / Disdolen)

✓ Approved

Uriach · PDE4A · Small Molecule

What is fosfosal?

fosfosal is a small molecule developed by Uriach. It is approved for therapeutic indications.

Drug Profile

Brand Namesfosfosal, Disdolen
CompanyUriach
Drug ClassSmall Molecule
Molecular TargetPDE4A, PDE4B, PDE4C, PDE4D, PTGS1, PTGS2
StatusApproved
Sources: ClinicalTrials.gov, Uriach

Mechanism of Action

Molecular Targets

fosfosal acts on 6 molecular targets:

PDE4Aphosphodiesterase 4A (PDE4, DPDE2)
PDE4Bphosphodiesterase 4B (DPDE4, PDEIVB)
PDE4Cphosphodiesterase 4C (DPDE1, PDE21)
PDE4Dphosphodiesterase 4D (PDE43, HSPDE4D)
PTGS1prostaglandin-endoperoxide synthase 1 (COX3, PCOX1)
PTGS2prostaglandin-endoperoxide synthase 2 (COX-2, COX2)
Want deeper analysis?Noah AI can explain complex mechanisms and compare to similar drugs.

Therapeutic Indications

fosfosal is developed for 3 unique indications across 3 therapeutic areas.

Therapeutic AreaConditionPhase
Gastrointestinal disordersAbdominal pain✓ Approved
Hepatobiliary disordersHepatitis✓ Approved
Musculoskeletal and connective tissue disordersMusculoskeletal pain✓ Approved

Related Research Articles

PubMedComputational biology and chemistry2025-05-24

In silico study of salicylic acid derivatives as inhibitors of Ebola proteins through molecular docking.

Rahimi Rezvan R, Solimannejad Mohammad M, Abnosi Mohammad Hossein MH

The Zaire Ebola virus is a highly virulent RNA virus that causes severe hemorrhagic fever in humans and nonhuman primates, with no effective treatments currently available. This study evaluates the inhibitory potential of six salicylic acid derivatives including aspirin, diflunisal, fendosal, fosfosal, salicylic acid, and salsalate; against three key Ebola virus receptor proteins through in-silico analysis. Molecular docking techniques have employed to model the interactions between these derivatives and the viral proteins VP24, VP35, and VP40. The results revealed that the salicylic acid derivatives demonstrated significantly stronger binding affinities to the VP35 receptor compared to other receptor proteins studied. Among the derivatives screened, those targeting the VP35 protein exhibited superior binding energy, glide energy, glide Emodel, glide Evdw, and glide ligand efficiency, alongside the lowest RMSD values. These findings suggest that salicylic acid derivatives hold promise as potential anti-Ebola therapies and warrant further investigation in clinical trials.

PMID 40409217
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PubMedFrontiers in molecular biosciences2020-08-09

High-Throughput Screening of a Functional Human CXCL12-CXCR4 Signaling Axis in a Genetically Modified S. cerevisiae: Discovery of a Novel Up-Regulator of CXCR4 Activity.

Murphy James W JW, Rajasekaran Deepa D, Merkel Janie J, Skeens Erin E et al.

CXCL12 activates CXCR4 and is involved in embryogenesis, hematopoiesis, and angiogenesis. It has pathological roles in HIV-1, WHIM disease, cancer, and autoimmune diseases. An antagonist, AMD3100, is used for the release of CD34+ hematopoietic stem cells from the bone marrow for autologous transplantation for lymphoma or multiple myeloma patients. Adverse effects are tolerated due to its short-term treatment, but AMD3100 is cardiotoxic in clinical studies for HIV-1. In an effort to determine whether Saccharomyces cerevisiae expressing a functional human CXCR4 could be used as a platform for identifying a ligand from a library of less ∼1,000 compounds, a high-throughput screening was developed. We report that 2-carboxyphenyl phosphate (fosfosal) up-regulates CXCR4 activation only in the presence of CXCL12. This is the first identification of a compound that increases CXCR4 activity by any mechanism. We mapped the fosfosal binding site on CXCL12, described its mechanism of action, and studied its chemical components, salicylate and phosphate, to conclude that they synergize to achieve the functional effect.

PMID 32766282
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PubMedChembiochem : a European journal of chemical biology2020-04-01

The Selectivity of Fosfosal for STAT5b over STAT5a is Mediated by Arg566 in the Linker Domain.

Gräb Julian J, Berg Thorsten T

Fosfosal is the O-phosphorylated derivative of salicylic acid, with documented clinical use as a prodrug for the treatment of inflammatory diseases. We recently discovered that fosfosal itself inhibits the protein-protein interaction domain, the SH2 domain, of the tumor-related transcription factor STAT5b. Here, we demonstrate that fosfosal is selective for STAT5b over its close homologue STAT5a. This selectivity is mediated by the STAT5b residue Arg566, located in the SH2 domain-adjacent linker domain. Our data provide further evidence for the role of the STAT linker domain in determining the activity of small molecules against the SH2 domain. We present a refined binding model for fosfosal and STAT5b, which can serve as the basis for the development of fosfosal-based STAT5b inhibitors.

PMID 32227557
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PubMedACS sensors2016-07-22

Detection of Alkaline Phosphatase Enzyme Activity with a CatalyCEST MRI Biosensor.

Daryaei Iman I, Ghaffari Mahsa Mohammadebrahim MM, Jones Kyle M KM, Pagel Mark D MD

Responsive CEST MRI biosensors offer good sensitivity and excellent specificity for detection of biomarkers with great potential for clinical translation. We report the application of fosfosal, a phosphorylated form of salicylic acid, for the detection of alkaline phosphatase (AP) enzyme. We detected conversion of fosfosal to salicylic acid in the presence of the enzyme by CEST MRI. Importantly the technique was able to detect AP enzyme expressed in cells in the presence of other cell components, which improves specificity. Various isoforms of the enzyme showed different Michaelis-Menten kinetics and yet these kinetics studies indicated very efficient catalytic rates. Our results with the fosfosal biosensor encourage further in vivo studies.

PMID 30246144
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PubMedACS chemical biology2011-07-30

Selective targeting of disease-relevant protein binding domains by O-phosphorylated natural product derivatives.

Gräber Martin M, Janczyk Weronika W, Sperl Bianca B, Elumalai Nagarajan N et al.

Phosphorylation-dependent protein binding domains are crucially important for intracellular signaling pathways and thus highly relevant targets in chemical biology. By screening of chemical libraries against 12 structurally diverse phosphorylation-dependent protein binding domains, we have identified fosfosal and dexamethasone-21-phosphate as selective inhibitors of two antitumor targets: the SH2 domain of the transcription factor STAT5b and the substrate-binding domain of the peptidyl-prolyl isomerase Pin1, respectively. Both compounds are phosphate prodrugs with documented clinical use as anti-inflammatory agents in humans and were discovered with a high hit rate from a small subgroup within the screening library. Our study indicates O-phosphorylation of appropriately preselected natural products or natural product derivatives as a generally applicable strategy for the identification of non-reactive and non-peptidic ligands of phosphorylation-dependent protein binding domains. Moreover, our data indicate that it would be advisable to monitor the bioactivities of clinically used prodrugs in their uncleaved state against phosphorylation-dependent protein binding domains.

PMID 21797253
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PubMedBiomaterials2005-11-02

Injectable and self-curing composites of acrylic/bioactive glass and drug systems. A histomorphometric analysis of the behaviour in rabbits.

González Corchón María Aránzazu MA, Salvado Manuela M, de la Torre Basilio José BJ, Collía Francisco F et al.

Injectable self-curing systems based on PMMA, phosphate-free bioactive glasses and the drug fosfosal, a phosphate derivative of salicylic acid with analgesic and moderate anti-inflammatory properties, have been tested in vivo to evaluate their biocompatibility. The model consisted of the injection of dough of cement into a defect created in the femur of rabbits, and the cure of the cement in situ after implantation. The biological response was studied in the short and long terms by macroscopic, radiological and histopathological examination, and quantitatively by histomorphometric and statistical analysis considering the most representative variables at the bone-cement interface: cement, bone marrow, newly formed bone and connective tissue. All bioactive formulations presented resorption of the cement at the end of the experiment in contrast to the control of PMMA, due to the presence of resorbable components. The presence or absence of the phosphate group added by the drug fosfosal influenced mainly on the new bone formation process. The cement formulated with bioactive glasses and in absence of fosfosal produced the maximum amount of neoformed bone at 2 weeks, and then it resorbed at 4 weeks to give a higher amount of neoformed bone at the end of the experiment, compared with the formulation containing only fosfosal. The presence of fosfosal and bioactive glass together affected the ossification process strongly. The osseous tissue was produced more gradually but it continuously increased giving rise to a more stable bone at the end of the experiment.

PMID 16260032
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