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artemisinin + amodiaquin (ASAQ / Winthrop / Coarsucam)

✓ Approved

DNDi · Small Molecule · Small Molecule

What is artemisinin + amodiaquin?

artemisinin + amodiaquin is a small molecule developed by DNDi. It is approved for therapeutic indications via oral (po).

Drug Profile

Brand NamesASAQ, Winthrop, Coarsucam
CompanyDNDi
Drug ClassSmall Molecule
RouteOral (PO)
StatusApproved
Sources: ClinicalTrials.gov, DNDi

Therapeutic Indications

artemisinin + amodiaquin is developed for 1 unique indication across 1 therapeutic area.

Therapeutic AreaConditionPhase
Infections and infestationsPlasmodium malariae infection✓ Approved

Related Research Articles

PubMedCommunications biology2026-07-17

ZDHHC12-dependent Nrf2 palmitoylation mediates the anti-ferroptotic and anti-inflammatory effects of artemisinin in mastitis.

Fan Zeqiu Z, Luo Yang Y, Zhang Zhenzhao Z, Cheng Feng F et al.

Artemisinin (ART) is known to alleviate inflammation in mastitis, but its effect on ferroptosis in mammary epithelial cells and the associated regulatory mechanisms has not been fully clarified. Here, we demonstrate that ART markedly attenuates inflammatory injury and ferroptosis in Staphylococcus aureus-induced mastitis models both in vivo and in vitro. ART treatment reduces iron accumulation and lipid peroxidation while restoring antioxidant capacity, accompanied by improved mitochondrial integrity. Mechanistically, ART upregulates the palmitoyltransferase ZDHHC12, which promotes palmitoylation of nuclear factor erythroid 2-related factor 2 (Nrf2) and facilitates its nuclear translocation. Activation of Nrf2 subsequently enhances heme oxygenase-1 (HO-1) signaling, leading to suppression of inflammation and ferroptosis. Collectively, these findings reveal that ART exerts protective effects against mastitis by activating the ZDHHC12/Nrf2/HO‑1 axis, highlighting ART as a potential therapeutic agent for mastitis through coordinated inhibition of inflammation and ferroptosis.

PMID 42463850
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PubMedbioRxiv : the preprint server for biology2026-07-17

A Multidimensional Analysis of the Bimodal Piperaquine Response in Plasmodium falciparum.

Kane John J, Schall Aubrey A, Checkley Lisa A LA, Shoue Douglas A DA et al.

Malaria remains a pressing global health challenge, with the continued emergence of resistance threatening the long-term efficacy of artemisinin-based combination therapies (ACTs). Piperaquine (PPQ), an important partner drug in artemisinin-based combination therapies exhibits a unique bimodal dose-response phenotype associated with reduced susceptibility, yet the biological mechanism underlying this phenotype remains unknown. This phenotype is strongly associated with mutations in pfcrt and copy number amplification of plasmepsin II/III ( pm II/III ). Given that plasmepsins play a central role in hemoglobin degradation within the blood stage parasite digestive vacuole, and that PPQ accumulates within this compartment and perturbs heme detoxification, this phenotype likely reflects alterations in fundamental biological processes alongside drug-specific effects. We used isogenic PPQ-resistant parasite clones differing only in pm II/III copy number to integrate phenotypes with metabolic changes, and transcriptional responses to ascertain the impact of genotype combinations on parasite response to PPQ. Across increasing PPQ concentrations, parasites with elevated pm II/III copy number exhibited distinct metabolic responses compared to single-copy parasites, specifically, an altered abundance of peptides derived from hemoglobin degradation, directly implicating a core biological pathway long associated with plasmepsin function. The combination of metabolic and transcriptional data with phenotypic measurements supports a model in which increased plasmepsin expression enhances the parasite's capacity to sustain hemoglobin digestion and associated metabolic activity under high PPQ concentrations. This points to a mechanistic basis for continued parasite survival, indicating that changes in hemoglobin processing within the digestive vacuole contribute to the bimodal response to PPQ. Molecular dynamics simulations further support a direct interaction between PPQ and PM II/III, as a mechanism by which these proteins impact PPQ response dynamics through both modulation of hemoglobin digestion and protein-drug interactions within the digestive vacuole.

PMID 42465291
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PubMedZhongguo xiu fu chong jian wai ke za zhi = Zhongguo xiufu chongjian waike zazhi = Chinese journal of reparative and reconstructive surgery2026-07-17

[Research progress on clinical transformation of Piezo1 in osteoarthritis].

Wang Yiyang Y, Wei Ning N, Zheng Zhanle Z

To review the role of the mechanosensitive ion channel Piezo1 in osteoarthritis (OA) pathogenesis and summarize recent advances in its clinical transformation as a potential therapeutic target. The recent domestic and international research literature was reviewed. Recent studies on Piezo1 in chondrocyte injury, inflammation, extracellular matrix degradation, and osteophyte formation were analyzed, along with Piezo1-targeted inhibitors, activators, and modulators. Piezo1 senses abnormal mechanical stress and mediates Ca 2+ influx, activating PI3K/AKT/mTOR and MAPK/ERK signaling pathways, thereby promoting chondrocyte apoptosis, impaired autophagy, and matrix degradation. Preclinical studies suggest that GsMTx4, Piezo1-siRNA, Dooku1, and artemisinin may confer chondroprotective effects, but their specificity, stability, delivery efficiency, and safety require further verification. Piezo1 is a critical link between mechanical stress and OA progression, representing a potential therapeutic target. Future research should focus on elucidating mechanisms, developing highly specific modulators and targeted delivery systems, and conducting rigorous preclinical and clinical studies to promote clinical transformation.

PMID 42464552
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PubMedbioRxiv : the preprint server for biology2026-07-17

Characterization of Sec14 domain-containing proteins in the malaria parasite Plasmodium falciparum.

Lauruol Florian F, Šťastný Dominik D, Fernandez-Murray J Pedro JP, McMaster Christopher R CR et al.

Malaria, of which the most virulent form is caused by Plasmodium falciparum parasites, remains a major global health burden. The appearance of resistance to first line treatments artemisinin-based therapies, emphasizes the need to identify new parasite vulnerabilities to develop new therapeutics. Phosphoinositides are central regulators of membrane identity, vesicular trafficking, and signaling, and their synthesis depends on tightly controlled phosphatidylinositol transfer by Sec14-like phosphatidylinositol transfer proteins in many eukaryotes, yet their roles in P. falciparum remain poorly defined. Here, we analyzed six P. falciparum Sec14 domain-containing proteins: PfSec14-1 (PF3D7_0626400), PfSec14-2 (PF3D7_0629900), PfSec14-3 (PF3D7_0717100), PfSec14-4 (PF3D7_0920700), PfSec14-5 (PF3D7_1007200), and PfSec14-6 (PF3D7_1127600). Domain organization segregates these proteins into a BNIP-2 and Cdc42GAP homology (BCH) subfamily (PfSec14-3, PfSec14-5) and a canonical Sec14 subfamily (PfSec14-1, PfSec14-2, PfSec14-4, PfSec14-6). Yeast complementation assays showed that PfSec14-1, PfSec14-4, and PfSec14-6 partially rescue growth of a temperature-sensitive sec14 mutant, suggesting phosphatidylinositol and phosphatidylcholine transfer activity. Gene disruption revealed that PfSec14-1 is important for asexual blood-stage proliferation, whereas PfSec14-2 is dispensable under standard culture conditions. In contrast, mislocalization of PfSec14-1 and PfSec14-4 using a knock-sideways approach did not impair asexual growth. Subcellular localization indicates distinct distributions for PfSec14-1, PfSec14-2, and PfSec14-4. Together, these findings reveal functional and spatial diversification of Sec14-like phosphatidylinositol transfer proteins in P. falciparum .

PMID 42465417
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PubMedInternational journal for parasitology. Drugs and drug resistance2026-07-16

High-throughput phenotypic screening identifies novel antimalarial scaffolds and target-associated chemotypes.

Ng'etich Japheth Kibet JK, Pravitasari Normalita Eka NE, Ishikawa Takeshi T, Kadofusa Naoya N et al.

The emergence and spread of artemisinin-resistant Plasmodium falciparum threaten recent progress in malaria control and highlight the urgent need for antimalarial agents with new mechanisms of action. Here, we performed a high-throughput phenotypic screening of the Nagoya Chemical Library, comprising 36,160 compounds. This yielded 1391 (3.8%) primary hits, further reduced by cytotoxicity profiling. Differential screening against wild-type 3D7 and transgenic 3D7-yDHODH parasites expressing yeast dihydroorotate dehydrogenase (DHODH) was done to identify mitochondrial electron transport chain inhibitors. This approach identified a compound with modest activity against parasite DHODH, confirmed by enzymatic assays with recombinant PfDHODH. A subset of 441 potent compounds with half-maximal concentration (EC50) < 6.5 μM was selected and profiled against the Dd2-derived multidrug-resistant panel. This analysis identified compounds likely targeting key parasite pathways, including phosphatidylinositol 4-kinase (PfPI4K) and P-type ATPase 4 (PfATP4). Chemical clustering of a selected subset of 350 compounds (<10 μM) revealed novel scaffolds with antiplasmodial potency that bear no structural resemblance to known antimalarial compounds. Collectively, these findings highlight novel chemotypes associated with validated antiplasmodial targets (PfDHODH, PfPI4K, and PfATP4) and uncover previously uncharacterized scaffolds with unknown targets. These compounds provide a foundation for further investigation of their mechanisms of action and optimization as potential antimalarial agents.

PMID 42456602
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PubMedFoods (Basel, Switzerland)2026-07-15

Artemisia annua and Its Derivatives Improve the Refrigerated Shelf Life of Nile Tilapia Fillets.

Aracati Mayumi Fernanda MF, Rodrigues Leticia Franchin LF, Oliveira Susana Luporini de SL, Rodrigues Romário Alves RA et al.

Artemisia annua contains artemisinin, a sesquiterpene lactone endoperoxide; artemether is a semisynthetic derivative of artemisinin that may offer potential advantages due to its redox-modulating and antimicrobial activities. These compounds have been associated with oxidative-stress modulation and microbial inhibition, making them promising candidates for experimental evaluation in nutritional and post-harvest quality studies. This study evaluated the effect of dietary supplementation with A. annua powder, artemisinin, and artemether on the refrigerated quality of Nile tilapia (Oreochromis niloticus) fillets. A total of 160 Nile tilapia were randomly assigned to four treatments: control (no additive), 1% A. annua powder, artemisinin (9.6 mg/kg feed), or artemether (9.6 mg/kg feed). After 30 days of feeding, 320 fillets were collected and stored under refrigeration at 4 °C. Samples were analyzed immediately after slaughter (day 0) and on days 7, 15, and 30. For each treatment group and sampling time, 20 fillets were used: 10 for microbiological evaluations, including counts of mesophilic and psychrotrophic bacteria, molds and yeasts, sulfite-reducing Clostridium, Enterobacteriaceae, coagulase-positive staphylococci, and coliforms; and 10 for physicochemical analyses, including pH, colorimetry, lipid oxidation through TBARS, and sensory evaluation. All supplemented treatments demonstrated improved microbial stability and lower TBARS values when compared with the control. Spoilage indicators such as discoloration, texture loss, and odor deterioration were also delayed. Artemether showed the most pronounced benefits, with lower microbial loads and oxidation indices for several evaluated parameters. These findings suggest that dietary supplementation with A. annua and its derivatives may help delay post-harvest quality deterioration of tilapia fillets during refrigerated storage.

PMID 42450505
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