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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

PubMedToxicology reports2026-10-06

Sub-acute dihydroxyacetone exposure alters mitochondria and induces cardiac strain.

Levi Hailey J HJ, Hernandez Arlet A, Hedlich-Dwyer Jenna J, Aggarwal Saurabh S et al.

Dihydroxyacetone (DHA), a carbohydrate detected in e-cigarette aerosols and used in sunless tanning products, is genotoxic and cytotoxic in various cell models. We previously demonstrated that inhaled DHA induced lung injury in A/J mice. Here, we evaluated cardiac effects of sub-acute DHA exposure in A/J mice and human Ac16 cardiomyocytes. Two weeks of DHA exposure significantly increased cardiac mitochondrial DNA (mtDNA) copy number and altered global longitudinal strain in both sexes. Ejection fraction and fractional shortening did not differ significantly after DHA exposure in either sex, though male mice showed increased ejection fraction and fractional shortening, while female mice decreased in both parameters. Male DHA-exposed mice also showed decreased body weight, while female mice body weight was unchanged. Plasma metabolic analyses, limited to female mice due to Flexivent analysis on the males, revealed significantly altered metabolic markers, including increased glucose levels and decreased resistin. To confirm mitochondrial DNA changes and DNA damage induction, we examined DHA exposure in the Ac16 cells sub-acutely exposed to DHA for 14 days. Sub-acute DHA exposure increased oxidative DNA lesions, without a significant increase in reactive oxygen species or mitochondrial content. mtDNA copy number was also increased in the sub-acutely exposed Ac16 cells. These results demonstrate that inhaled DHA alters cardiac cells and induces early cardiac tissue and cell changes, in addition to its lung effects, suggesting that the e-liquid oxidation products pose inhalation-related health risks.

PMID 42835281
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PubMedPLoS pathogens2026-09-29

Metabolic regulation of the carbonyl stress pathway and methylglyoxal in Lyme disease and relapsing fever spirochetes.

Drecktrah Dan D, Hall Laura S LS, Cheff Britney B, Richards Crystal C et al.

The carbonyl stress pathway in bacteria is mediated by the enigmatic metabolite methylglyoxal and is thought to be activated in response to cellular carbohydrate and phosphate imbalance. Methylglyoxal, produced from dihydroxyacetone phosphate by methylglyoxal synthase, covalently modifies nucleophilic groups of amino acid residues, such as lysine, arginine and cysteine, to yield advanced glycation end products. In this work, we have identified several environmental signals, including glycerol and peptides, which activate carbonyl stress in the Lyme disease spirochete Borrelia (Borreliella) burgdorferi. We establish that methylglyoxal production and protein glycation is dependent on the mgsA gene (bb0364) product and show that this pathway is active in Lyme disease spirochetes, but not relapsing fever Borrelia or in B. mayonii. Furthermore, we have investigated the role of carbonyl stress in the tick-mouse model of Lyme disease and provide evidence that production of methylglyoxal and glycation of proteins is not necessarily lethal, as previously believed, at least in Lyme disease spirochetes. Finally, we show that expression of the B. burgdorferi mgsA and carbonyl stress pathway in the relapsing fever spirochete B. hermsii significantly reduces the peak level of spirochetemia during the relapse phase of murine infection. Together, our results identify a new post-translation modification system in Lyme disease spirochetes that appears to be important in governing the lifestyle of this pathogen and seems to be selected against in spirochetes that reach high numbers in the blood.

PMID 42809612
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PubMedMethods in enzymology2026-09-28

Use of dihydroxyacetone synthase for the assimilation of methanol in E. coli.

De Simone A A, Malfoy T T, Peiro C C, Heux S S

Dihydroxyacetone synthase (Das) is a key enzyme of the xylulose monophosphate (XuMP) pathway, catalysing the assimilation of formaldehyde in methylotrophic yeasts. In this study, we first performed a systematic screening of twenty-five Das variants in combination with a methanol dehydrogenase (Mdh) from Acinetobacter gerneri to identify the Das variants supporting the most efficient methanol assimilation.13C-methanol labelling experiments revealed marked differences in 13C incorporation into central carbon metabolism among the various Das variants and enabled the identification of the Pichia angusta Das variant as the most efficient candidate. To further investigate Das activity in vitro, a coupled enzymatic assay was developed using glycerol dehydrogenase as a reporter via NADH oxidation. Initial enzymatic assays revealed significant background activity, prompting optimization of purification and assay conditions. Implementation of higher ionic strength buffers, protease inhibition, increased wash stringency, and stepwise imidazole elution substantially improved enzyme purity and assay specificity, enabling reliable measurement of P. angusta Das activity. Finally, to directly demonstrate the carbon transfer catalyzed by P. angusta Das, purified enzyme was assayed with 13C-formaldehyde and xylulose-5-phosphate, and reaction products were analyzed by 1H NMR spectroscopy. 13C incorporation was detected exclusively in dihydroxyacetone, confirming that Das catalyzes a thiamine pyrophosphate-dependent transfer of a C1 unit from formaldehyde to xylulose-5-phosphate, yielding equimolar amounts of dihydroxyacetone and glyceraldehyde-3-phosphate. This provides the first direct in vitro demonstration of Das transketolase activity using purified enzyme and native substrates, and establishes a robust framework for studying and engineering synthetic methanol assimilation pathways.

PMID 42805705
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PubMedMethods in enzymology2026-09-28

Protein engineering of formolase for the synthesis of 1,3-dihydroxyacetone from formaldehyde.

Tan Zijian Z, Zhang Ruke R, Liu Haifeng H, Zhu Leilei L

Formaldehyde is an attractive one-carbon building block for sustainable biomanufacturing, but efficient conversion of formaldehyde into higher-value chemicals remains challenging. Formolases, a class of engineered thiamine pyrophosphate-dependent enzymes, catalyze the condensation of formaldehyde to produce glycolaldehyde or 1,3-dihydroxyacetone (DHA), yet their catalytic performance is often insufficient for practical application. This chapter presents a workflow for engineering a benzoylformate decarboxylase (BFD)-derived formolase through a channel-modulating helix strategy. The protocol covers target identification by homologous structural motion analysis and substrate-channel mapping, construction of site-saturation mutagenesis libraries, high-throughput screening in 96-well plates under low-formaldehyde conditions (20 mM), and biochemical characterization of positive variants. Detailed procedures are provided for primer design, library construction, culture and expression in microplates, DHA detection, and kinetic evaluation. This workflow offers a practical platform for improving formolase performance and may be adapted for engineering other channel-dependent enzymes.

PMID 42805703
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PubMedMethods in enzymology2026-09-28

High-throughput engineering of glycolaldehyde synthase for enhanced formaldehyde conversion to C2 and C3 products via mass spectrometry-based screening.

Luo Yizhou Y, Fu Lihao L, Lin Peikai P, Si Tong T et al.

One-carbon (C1) biomanufacturing offers a sustainable route for producing value-added chemicals. Glycolaldehyde synthase (GALS), a thiamine pyrophosphate (TPP)-dependent enzyme engineered from benzoylformate decarboxylase of Pseudomonas putida, catalyzes the condensation of formaldehyde (FALD) to yield the C2 and C3 platform chemicals glycolaldehyde (GALD) and dihydroxyacetone (DHA). However, its industrial application is constrained by low catalytic efficiency and the lack of high-throughput screening (HTS) methods. This chapter presents a comprehensive HTS workflow for engineering GALS variants. We first detail the construction of an optimized Escherichia coli chassis (BL21(DE3)-Δ6) via CRISPR/Cas9-mediated deletion of six endogenous reductase genes to minimize competing FALD consumption. Next, we present the development of a mass spectrometry (MS)-based assay using 3-methyl-2-benzothiazolinone hydrazone hydrochloride (MBTH) derivatization coupled with RapidFire-MS/MS for simultaneous quantification of GALD and DHA. Integrating this MS assay with a robotic biofoundry enables automated screening of site-saturation mutagenesis (SSM) libraries at a throughput of ∼10 s per sample. Finally, we establish validation protocols for candidate variants, including enzyme purification and kinetic characterization using microplate-based colorimetric assays. The established methodology is readily adaptable to the engineering of diverse aldehyde-producing TPP-dependent enzymes.

PMID 42805702
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PubMedACS omega2026-09-18

Influence of Temperature on Reaction Pathways in Fructose Conversion over Mixed Oxide Catalysts Based on Ce and Nb.

Pryston Dhara Beatriz de Amorim DBA, Martins Thatiane Veríssimo Dos Santos TVDS, Dos Santos Jailma Barros JB, Ferreira Daniel Santos Vilela DSV et al.

The influence of temperature on the product distribution during fructose conversion was systematically investigated using Ce-(P), Nb-(P), CeNb5-(P), CeNb15-(P), and CeNb25-(P) materials prepared by the Pechini method. Reactions were performed in aqueous medium for 2 h at temperatures ranging from 130 to 160 °C. Increasing temperature enhanced fructose conversion but also modified the relative contributions of dehydration, fragmentation, and consecutive degradation pathways. Nb-(P) reached the highest fructose conversion, increasing from 17.6% at 130 °C to 67.9% at 160 °C, but also exhibited a greater contribution from unidentified and degradation products under the most severe conditions. In contrast, the Ce-Nb mixed oxides, particularly CeNb15-(P) and CeNb25-(P), more effectively directed the identified soluble products toward 5-hydroxymethylfurfural (5-HMF), while limiting some competing pathways. The formation of C3 compounds, including dihydroxyacetone and pyruvaldehyde, indicates the occurrence of C-C bond cleavage reactions, whose contribution increased with temperature and depended on material composition. The observed product distributions result from the combined influence of temperature, acid-site nature, concentration, strength, and accessibility, together with the redox properties of the Ce containing materials. These findings demonstrate that the principal contribution of the studied oxides lies in their catalyst dependent modulation of the fructose reaction network rather than in the effect of temperature alone.

PMID 42756796
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