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dihydroxyacetone (Nigrantil)

✓ Approved

Vinas · Small Molecule · Small Molecule

What is dihydroxyacetone?

dihydroxyacetone is a small molecule developed by Vinas. It is approved for therapeutic indications.

Drug Profile

Brand NamesNigrantil
CompanyVinas
Drug ClassSmall Molecule
StatusApproved
Sources: ClinicalTrials.gov, Vinas

Therapeutic Indications

dihydroxyacetone is developed for 1 unique indication across 1 therapeutic area.

Therapeutic AreaConditionPhase
Skin and subcutaneous tissue disordersVitiligo✓ Approved

Related Research Articles

PubMedEssays in biochemistry2026-07-24

Distribution of lactone-signaling system for expression of secondary metabolite biosynthetic gene clusters in Streptomyces species.

Teshima Aiko A, Inada Kuninobu K, Arakawa Kenji K

Many Streptomyces species have a signaling-molecule/receptor system for induction of secondary metabolite biosynthetic gene clusters (BGCs). Signaling molecules hitherto discovered and studied contain five-membered heterocycles, and are classified into three groups, including γ-butyrolactones, γ-butenolides, and furans. These molecules except for avenolide-type are biosynthesized by enzymes harboring an AfsA tandem repeat domain. These enzymes (AfsA homologs) catalyze a transfer of β-ketoacyl moiety to the hydroxyl group of dihydroxyacetone phosphate. Alignment of 59 afsA homolog genes showed that 86% (51/59) of them located adjacent to their possible signaling-molecule receptor genes, which reminds us to readily predict their signaling-molecule/receptor system for expression of BGCs. Apparent exception is the case of afsA-arpA system in Streptomyces griseus, whose distance was around 3.91 Mb. Understanding of the signaling-molecule/receptor system may lead to a practical genome mining strategy to awaken silent BGCs through derepression of transcription using the cognate ligands, signaling molecules.

PMID 42494319
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PubMedNature communications2026-07-21

Towards an enzyme cascade synthesis of the bulk chemical acrylic acid.

Zhao Haodong H, Wang Chunying C, Zhang Shiqing S, Wang Qian Q et al.

Acrylic acid is a bulk chemical predominantly produced via fossil-based processes. Here, we repurpose and engineer a thiamine diphosphate (ThDP)-dependent enzyme to catalyze direct H2PO4- elimination from dihydroxyacetone phosphate (DHAP) for acrylic acid synthesis. Quantum chemical calculations reveal the catalytic mechanism involving isomerization, enol-ThDP intermediate formation, H2PO4- elimination, and hydrolysis. Using an automated high-throughput screening platform, we perform directed evolution and obtain a 13.6-fold improved variant, designated acrylic acid synthase (AAS). We establish an enzymatic methanol-to-acrylic acid (MAAP) pathway, achieving a titer of 4.3 g L-1, a productivity of 268.9 mg L-1 h-1, and 99.5% conversion. This work establishes a high-efficiency biomanufacturing paradigm for bulk acrylic acid, and expands the catalytic repertoire of ThDP-dependent enzymes for sustainable one-carbon conversion.

PMID 42477336
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PubMedAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026-07-17

TPI1 Loss Triggers a Metabolite-Driven Mitochondrial Redox Vulnerability via the SARM1-cADPR-Ca2+ Axis.

Liu Chunyu C, Wu Shun S, Wang Chuang C, Zhou Zirui Z et al.

Cellular senescence is a stable cell cycle arrest program with important therapeutic implications in cancer, yet how metabolic perturbations are translated into redox-dependent senescence remains incompletely understood. Here, we identify triosephosphate isomerase 1 (TPI1) as a critical regulator of senescence in clear cell renal cell carcinoma (ccRCC) through a customized CRISPR-Cas9 metabolic screen. TPI1 depletion induces a robust senescence phenotype characterized by mitochondrial redox imbalance, DNA damage, and stable growth arrest. Mechanistically, loss of TPI1 leads to accumulation of dihydroxyacetone phosphate (DHAP), which engages a SARM1-dependent signaling pathway, resulting in increased cyclic ADP-ribose (cADPR) production and intracellular Ca2+ release. This cADPR-Ca2+ axis drives mitochondrial ROS (mtROS) generation, thereby promoting DNA damage and activation of the p53-p21 pathway to enforce senescence. Pharmacological or genetic attenuation of calcium signaling, or mitochondrial ROS partially rescues these phenotypes, indicating that calcium-dependent redox stress is required for senescence induction. Importantly, this metabolic-redox signaling cascade is conserved across multiple cancer types. Collectively, our findings define a previously unrecognized TPI1-SARM1-cADPR-Ca2+ axis that links glycolytic metabolite accumulation to mitochondrial redox stress and cellular senescence, highlighting a metabolite-driven redox vulnerability that may be therapeutically exploitable in cancer.

PMID 42467906
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PubMedNanoscale2026-07-16

Yolk-shell microenvironment engineering enables Au/CuO@Void@mSiO2 catalysts with high activity and cycling stability for glycerol oxidation to 1,3-dihydroxyacetone.

Zheng Tao T, Wang Fei F, Yang Yukun Y, Zhang Xiaoli X et al.

The selective oxidation of glycerol, a renewable by-product of biodiesel production, to 1,3-dihydroxyacetone (DHA) offers a green and sustainable pathway for biomass upgrading, yet the development of catalysts that simultaneously achieve high activity and long-term cycling stability remains challenging. In this work, Au/CuO@Void@mSiO2 yolk-shell nanoparticles with engineered microenvironments were synthesized via an improved Stöber method combined with an adsorption-reduction strategy, and constructed as highly active and cycling-stable catalysts for base-free glycerol oxidation to DHA. A series of samples were prepared by adjusting the dosage of silica source, template, and precursor to tailor yolk-shell microenvironments. Among the prepared samples, the optimized catalyst, Au/CVmS-10, delivered 92.9% glycerol conversion with 91.3% selectivity toward DHA at 100 °C within 2 h. Notably, it maintained 89.1% conversion and 90.0% selectivity after five cycles, outperforming all previously reported base-free catalysts. Comprehensive characterization and analyses revealed that yolk-shell microenvironment engineering endowed the catalysts with excellent structural stability, high-specific-surface-area core-shell structure, rapid mass transfer, and enriched adsorbed oxygen species, as well as precisely tunable shell thickness, pore structure and interlayer void space, thus retaining outstanding catalytic performance throughout repeated cycling tests. This work highlights the microenvironment regulation within yolk-shell architectures as a key factor for enhancing both activity and durability in glycerol valorization.

PMID 42461026
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PubMedClinical case reports2026-07-14

Intravenous Dihydroxyacetone as Adjunctive Therapy in Aluminum Phosphide Poisoning: A Case Series.

Niknahad Hossein H, Heidari Reza R, Hosseini Leila L, Yazdani Shayan S et al.

In three patients with aluminum phosphide poisoning, intravenous dihydroxyacetone (DHA) was added to standard supportive care. Improvement in metabolic acidosis and hemodynamic status was temporally associated with DHA administration. Controlled studies are needed to determine efficacy and safety.

PMID 42445459
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PubMedBiochemical and biophysical research communications2026-07-14

Crystal structure of a fungal dihydroxyacetone kinase reveals a non-canonical ATP-binding site.

Wei Hongli H, Chen Yangyang Y, Zhang Fan F, Li Qian Q et al.

Dihydroxyacetone kinase (DAK) catalyzes the ATP-dependent phosphorylation of dihydroxyacetone (DHA) and is an important enzyme in artificial starch synthesis. Here, we report the crystal structure of a methylotrophic yeast DAK from Komagataella phaffii (formly Pichia pastoris, PpDAK). ATP was observed at a non-canonical site distinct from the canonical bacterial ATP-binding pocket. Docking further suggested that the canonical pocket remains accessible, indicating flexibility in ATP recognition. Sequence and phylogenetic analyses show that PpDAK clusters within a distinct methylotrophic yeast lineage and that residues surrounding the non-canonical ATP-binding site are conserved among methylotrophic yeasts. In addition, Mg2+ ions were identified in some substrate-binding pockets and docking suggested substantial overlap between Mg2+ and the predicted DHA-binding position. Together, these findings provide structural insights into ATP recognition in fungal DAKs and a framework for future functional studies and enzyme engineering.

PMID 42442090
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