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dihydroxyacetone (Nigrantil)

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Vinas · 小分子 · 小分子

什么是 dihydroxyacetone?

dihydroxyacetone 是一种小分子,由Vinas研发。该药已获批,用于治疗相关适应症。

药物档案

商品名Nigrantil
公司Vinas
药物类别小分子
状态Approved

治疗适应症

dihydroxyacetone 针对 1 个适应症,涉及 1 个治疗领域。

治疗领域疾病/病症分期
Skin and subcutaneous tissue disordersVitiligo✓ Approved

相关研究文献

PubMedNanoscale2026-09-08

Zn vacancy-engineered Au-based catalysts for the selective oxidation of glycerol to 1,3-dihydroxyacetone.

Shi Xiaoqing X, Wang Lei L, Tian Zhaowei Z, Wang Si S et al.

The efficient catalytic oxidation of biomass to produce high-value chemicals has become a major focus of current research. In this work, we report an Au/ZnvAl-MMO catalyst rich in zinc vacancies, which exhibits excellent catalytic performance in the selective oxidation of glycerol (conversion of ∼97.8% and a DHA yield of ∼80.4%). Experimental studies [X-ray photoelectron spectroscopy (XPS), X-ray absorption fine structure (XAFS), and in situ CO diffuse reflectance infrared Fourier transform spectroscopy (CO-DRIFTS)] indicate that the introduction of Zn defects leads to electron enrichment on O atoms adjacent to Zn vacancies, which promotes the reduction of Au and simultaneously forms unique Auδ+-O-Znv interfacial sites. Kinetic experiments further demonstrate that catalysts with a higher Au0 content exhibit a stronger ability to activate O2, resulting in significantly enhanced glycerol conversion. Combined in situ Fourier-transform infrared (FT-IR) spectroscopy and density functional theory (DFT) calculations reveal that the secondary O-H bond of glycerol preferentially adsorbs and activates at the Zn sites of the Auδ+-O-Znv interfacial structure. Meanwhile, the interfacial Auδ+ species facilitate the storage and migration of OH- and OOH- species. In addition, the electron-rich interfacial oxygen atoms establish stronger hydrogen-bonding interactions with the secondary O-H and β-H groups, thereby synergistically promoting the cleavage of both the secondary O-H and β-H bonds. This work not only offers important insights into the oxidation pathways of polyols, but also provides a simple and effective strategy for the efficient catalytic oxidation of biomass to produce high-value chemicals.

PMID 42706993
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PubMedWorld journal of microbiology & biotechnology2026-08-29

Advances in glycerol metabolism comprehension in yeasts: from regulation to metabolic engineering strategies.

Fonseca Juliana Silva Carneiro JSC, da Silveira Wendel Batista WB

Glycerol is a polyol that can be produced either chemically from oils or propylene, or biologically by yeasts, mainly under osmotic stress. Currently, glycerol is an abundant byproduct generated during biodiesel manufacturing that can be used as substrate in fermentative processes. Its efficient assimilation varies widely among yeast species; therefore, understanding the regulation of both transport and catabolism is pivotal for optimizing biotechnological processes based on this carbon source. This review addresses current knowledge on the regulatory networks controlling glycerol metabolism in yeasts, compassing transport mechanisms, metabolic pathways, transcriptional control and enzyme regulation. We highlight the distinct roles of the Stl1p symporter and Fps1p aquaglyceroporin in mediating glycerol flux across the plasma membrane, as well as the species-specific reliance on either the glycerol-3-phosphate (G3P) or dihydroxyacetone (DHA) pathway for glycerol assimilation. Classical biochemical studies have shown that glycerol catabolic enzymes are tightly regulated by carbon source availability, osmotic conditions, and feedback inhibition. Recently, transcriptomic and genetic analyses, particularly in Yarrowia lipolytica, show that the glycerol metabolism is governed by complex interactions between catabolite repression, nutrient signaling, and metabolic intermediates such as G3P, which acts as a key regulatory signal. Despite significant advances, regulatory mechanisms remain elusive in most non-conventional yeasts, underscoring the need for broader comparative studies. In addition, we review major metabolic engineering strategies aimed at enhancing glycerol utilization or redirecting carbon flux toward targeted bioproducts, emphasizing how mechanistic insights into glycerol metabolism and its regulation can guide the development of engineered strains with improved features for industrial applications. Lastly, we pointed out promising avenues for future research and biotechnological innovation.

PMID 42667578
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PubMedJournal of fungi (Basel, Switzerland)2026-08-26

Role of Glycerol-3-Phosphate Dehydrogenase in the Development, Pathogenicity, and Glycerol Biosynthesis of Aspergillus flavus.

Zhang Liurong L, Zhao Jiaru J, Lin Hongyi H, Wu Shaoze S et al.

Aspergillus flavus, a ubiquitous phytopathogen, produces mycotoxins, especially aflatoxin B1 (AFB1), and infects crops worldwide. Glycerol-3-phosphate dehydrogenase (G3PDH) is a key enzyme in the glycerol synthesis and metabolic pathway catalyzing the reversible conversion reaction between glycerol-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). However, the biological function of G3PDH in A. flavus remains uncharacterized. In this study, the glycerol-3-phosphate dehydrogenase GfdA and GfdB recombinant proteins of A. flavus were expressed, and the enzymatic activity of the GfdA protein was successfully determined. Subsequently, single-gene knockout strains (ΔgfdA, ΔgfdB), double-gene knockout strains (ΔgfdAΔgfdB) and their corresponding complemented strains (gfdAC, gfdBC) were constructed by a homologous recombination method to explore the biological functions of these two genes in A. flavus. The phenotypic analyses revealed that although both gfdA and gfdB encoded glycerol-3-phosphate dehydrogenases, gfdA plays major roles in colony growth, conidiation, sclerotium formation, crop infection and osmotic stress tolerance in A. flavus. Notably, the performance of the ΔgfdAΔgfdB strains is almost similar to that of the ΔgfdA strain. Biochemical assays demonstrated that the intracellular glycerol content increased significantly in all mutants compared to the wild type (WT) under both normal and osmotic stress conditions. Furthermore, we found that exogenous glycerol supplementation rescued the growth defect of the ΔgfdA and ΔgfdAΔgfdB strains. Taken together, GfdA is important for glycerol synthesis, while GfdB is functionally redundant with respect to GfdA. This study preliminarily explores the main biological functions of GfdA and GfdB, providing a theoretical basis for the study of glycerol anabolic pathways of A. flavus and also offering novel insights into the development of strategies to control aflatoxin contamination.

PMID 42646137
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PubMedCells2026-08-13

Distinct Metabolomic and Proteomic Signatures of Early Brain Damage Triggered by the Entrance Plateau Versus the Spread-Out Bragg Peak of Proton Radiation.

Liao Keman K, Xu Fei F, Gao Yunsheng Y, Jiang Xuming X et al.

Proton therapy spares normal tissues better than photon therapy, potentially reducing toxicity while maintaining tumor control. However, challenges remain due to variations in proton dose distribution, particularly at the distal edge of the spread-out Bragg peak (SOBP); for organs at risk, such variation is crucial. We evaluated the biological effects by comparing two positions of the proton profile, the entrance plateau (EP) and SOBP, in a murine model and investigated distinct metabolomic and proteomic signatures. Mice exposed to the EP beam segment (LETd = 0.8 keV/µm) exhibited less weight reduction than their SOBP-irradiated counterparts (LETd = 2.6 keV/µm). Two hours post-irradiation, the SOBP caused more severe DNA damage in the hippocampus and thalamus. Hematoxylin and eosin staining revealed eosinophil aggregation in both groups, with more surviving neurons in the EP group. Metabolomic profiles differed more between the EP and SOBP groups at 2 h than at 3 days post-irradiation. Relative to EP, SOBP irradiation at 2 h increased fructose-1,6-bisphosphate (FBP), dihydroxyacetone phosphate (DHAP), and inosine but decreased prostaglandin F2α; subsequently, proteomic analysis at day 3 showed that calcium signaling, NF-κB, and endocytosis pathways were enriched in the SOBP group. Combined multi-omics analysis further demonstrated that SOBP irradiation significantly activated the pentose phosphate pathway, purine metabolism, and phospholipase D signaling, while concurrently suppressing arachidonic acid metabolism. Our findings underscore the need for early detection of proton-induced brain toxicity and demonstrate that the higher-LET SOBP segment causes more severe damage than the EP. Targeting these dysregulated multi-omics pathways may offer a promising strategy for mitigating radiation-induced brain injury during proton therapy.

PMID 42587791
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PubMedFood science & nutrition2026-08-06

Antiglycation of Insulin by Selected Six Bioactive Peanut Sprout Stilbenoids and Demonstration of Methylglyoxal-Mediated Biphasic Insulin Glycation by O-Phenylenediamine Derivatization.

Chiu Po-Chang PC, Lin Shu-Mei SM, Li Yu-Jang YJ, Lo Chih-Yu CY et al.

Protecting insulin molecules from glycation by the dietary ingredients is critical to alleviate diabetes-associated metabolic complications. Six peanut sprout stilbenoids were selected for antiglycation determination with bovine insulin mediated by methylglyoxal (MG), glucose, and fructose. Monitoring at 215 nm via HPLC analysis revealed that all test compounds exhibited inhibitory activities with structure-activity dependency, among those arachidin-3 performing the most potent efficacy (p < 0.05). Notably, a biphasic dose-response was observed, indicating that MG-mediated insulin modification increased as MG concentrations decreased from 500 to 5 mM and then declined as MG concentrations dropped to 0.05 mM. This was supported by insulin band-intensity changes shown in Tricine SDS-PAGE pattern. O-phenylenediamine (OPD) was utilized as a trapping probe to form MG-OPD adducts for characterization and isolation. In high-MG concentrations, a novel intermediate: 2-(hydroxymethyl)-1,2,3,4-tetrahydroquinoxaline-2,3-diol (2HMQL) was isolated, identified and merited to speculate its precursor compounds existing in the MG equilibrium complex with less reactive hydrates or tautomers (e.g., dihydroxyacetone and/or hydroxypyruvaldehyde) which protect insulin integrity from glycation. It is of merit to demonstrate that identification of 2HMQL provides a proposed equilibrium mechanism to elucidate the biphasic MG-mediated insulin glycation.

PMID 42559065
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PubMedThe FEBS journal2026-08-05

Common pathways and outliers in glucose catabolism across Trypanosomatidae.

Opperdoes Fred R FR, Alencar Mayke B MB, Silber Ariel M AM, Škodová-Sveráková Ingrid I et al.

Glucose catabolism in trypanosomatids differs significantly from that in most other eukaryotes. Here, the first few enzymes of the pathway are all located inside glycosomes, that is, the peroxisome-like microbodies uniquely present in the Kinetoplastida and Diplonemida of the Euglenozoa. Glycosomal AMP/ADP/ATP and NAD(H)+ pools cannot freely equilibrate with their corresponding cytosolic pools, and any ATP and NAD+ consumed within the organelles have to be regenerated inside to maintain the redox balance and glycolytic flux. Analyses of the reported end-products of both aerobic and anaerobic glucose catabolism experiments in various trypanosomatids have revealed that the ability to maintain the intra-glycosomal ATP/ADP energy balance and NAD+/NADH redox balance is essentially limited to three pathways. 1) Under aerobic conditions, glycosomal NADH is preferably reoxidized indirectly by molecular oxygen via a dihydroxyacetone phosphate/glycerol-3-phosphate shuttle which links to the mitochondrial respiratory chain, where either an alternative oxidase or a cytochrome oxidase functions as terminal oxidases. 2) Under oxygen starvation or limited activity of enzymes of the DHAP/G3P shuttle, glycosomal NADH is reoxidized by a redirection of part of the cytosolic PEP towards the glycosome, where it is reduced to succinate. 3) A succinate/fumarate/malate cycle permits an exchange of succinate and malate between the glycosome/cytosol and the mitochondrion via a mitochondrial dicarboxylate carrier, whereby succinate is oxidized to fumarate by the mitochondrial succinate dehydrogenase (complex II). In parallel, trypanosomatids have evolved various pathways to form sufficient ATP to satisfy their energy requirements. Some trypanosomatids survive true anaerobiosis through pyruvate dismutation or fermentation of propionic acid.

PMID 42552839
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