Synonyms:L(+)-Ascorbic acid;L-Ascorbic acid（C);(R)-5-((S)-1,2-Dihydroxyethyl)-3,4-dihydroxyfuran-2(5H)-one;L-Ascorbic acid;L-Threoascorbic acid,Antiscorbutic factor,Vitamin C;L-Ascorbic Acid;
99%min *data from raw suppliers
Ascorbic Acid *data from reagent suppliers
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There total 75 articles about L(+)-Ascorbic acid which guide to synthetic route it. The literature collected by LookChem mainly comes from the sharing of users and the free literature resources found by Internet computing technology. We keep the original model of the professional version of literature to make it easier and faster for users to retrieve and use. At the same time, we analyze and calculate the most feasible synthesis route with the highest yield for your reference as below:
Reference yield: 94.0%
Reference yield: 83.0%
Reference yield: 83.0%
(3R,4R,5S)-3,4,5,6-Tetrahydroxy-2-oxo-hexanoic acid methyl ester
The research focuses on the AlkB domain of the mammalian ABH8 protein, which is part of the AlkB family of nonheme iron/α-ketoglutarate (aKG)-dependent dioxygenases. The study aimed to investigate the biochemical activity of ABH8, particularly its role in RNA modification. The researchers hypothesized that ABH8 could modify tRNAs through a controlled methylation/demethylation process. Through a series of experiments, they discovered that the AlkB domain of ABH8 catalyzes the hydroxylation of 5-methoxycarbonylmethyluridine (mcm5U) at the wobble position of tRNA, converting it into 5-(S)-methoxycarbonylhydroxymethyluridine ((S)-mchm5U). This modification was found to be specific to ABH8 and required the presence of iron(II) and aKG cofactors. The chemicals used in the process included iron and aKG as cofactors, l-ascorbic acid, and EDTA for quenching the reaction. The conclusions of the study suggest that ABH8 may play a role in regulating RNA function and could have implications in cancer progression, as it was previously shown to affect cancer cells. The findings also expand the understanding of the AlkB family of proteins, which were previously known for their demethylation activities, to include modification functions on nucleic acids.
This research presents the development of a heterogeneous palladium catalyst supported by a polymerized functional ionic liquid for the reductive homocoupling of aryl halides. The purpose of the study was to create a recyclable catalyst that could selectively catalyze the formation of biaryls, which are important building blocks in pharmaceuticals and agrochemicals, under mild conditions. The researchers synthesized a homopolymer of 3-(cyanomethyl)-1-vinylimidazolium hexafluorophosphate and used it to support Pd nanoparticles, resulting in the Pd@poly-CN-PF6 catalyst. This catalyst was found to efficiently catalyze the homocoupling reactions of aryl halides in water at 100°C with good yields. The catalyst could be recycled and reused multiple times with only a slight loss in activity, which was attributed to palladium leaching at high temperature and aggregation of palladium nanoparticles. Key chemicals used in the process included 1-vinylimidazole, 2-chloroacetonitrile, potassium hexafluorophosphate, azodiisobutyronitrile (AIBN), and sodium borohydride (NaBH4) for the synthesis of the polymer and the Pd nanoparticles, as well as aryl halides, NaOH, and ascorbic acid in the catalytic reactions.
The research focused on exploring the reactivity of L-ascorbic acid in the context of the Michael addition to cyclic enones, specifically 2-cyclohexenone and 2-cyclopenten-1-one. The purpose was to investigate the potential of L-ascorbic acid as a catalytic agent in synthesizing biologically active compounds, such as 2-(3'-cyclohexyl)-3-keto-L-gulonolactone and 2-(3'-cyclopentyl)-3-keto-L-gulonolactone. The study concluded that the addition of concentrated hydrochloric acid significantly enhanced the reaction efficiency, leading to the successful formation of the desired products. The research highlighted the importance of the electrophilic nature of the cyclic enones in facilitating the reaction, demonstrating that L-ascorbic acid can effectively serve as a donor in Michael addition reactions under acidic conditions.
The study presents the development of a series of platinum(IV) prodrugs, specifically designed to enhance interaction with human serum albumin (HSA) for drug delivery purposes. The prodrugs were synthesized by asymmetrically functionalizing the axial ligands to mimic the features of a fatty acid, with the aim of improving cellular uptake and cytotoxicity. The lead compound, 4e, which has a hexadecyl chain, demonstrated a significant therapeutic potential due to its ability to form a tight, non-covalent complex with HSA (complex 7), enhancing its stability in blood and reducing the rate of reduction by ascorbate. The study involved platinum(IV) complexes with varying aliphatic tail lengths, including 4a, 4b, 4c, 4d, and 4e, which were used to investigate the impact of lipophilicity on cellular uptake and cytotoxicity. Other chemicals used included cisplatin as a reference compound, succinic anhydride, isocyanate reagents for the synthesis of the prodrugs, and ascorbate as a biological reductant to study the reduction of the Pt(IV) prodrugs. The purpose of these chemicals was to create a novel class of anticancer prodrugs with improved properties, such as enhanced stability, reduced side effects, and potentially increased efficacy.
The research aims to develop and investigate BODIPY-peptide conjugates that target the extracellular domain of the epidermal growth factor receptor (EGFR), a receptor overexpressed in various cancers, particularly colorectal cancer (CRC). The purpose of this study is to prepare and examine the binding ability of three BODIPY-peptide conjugates to EGFR, with the ultimate goal of enhancing tumor cell specificity for cancer therapy and early detection. The researchers used copper-catalyzed click chemistry to conjugate alkynyl-functionalized BODIPY dyes with peptides modified to include an azide group, resulting in high-yield conjugates. The chemicals used in the process include BODIPY dyes 1 and 2, azido-peptides L1.5 and cycloL1.1, copper(I) sulfate pentahydrate (CuSO4·5H2O), copper(0), L-ascorbic acid, and various solvents such as tetrahydrofuran (THF) and water. The conjugates were tested for their binding affinity to EGFR using surface plasmon resonance (SPR) and for their cellular uptake and cytotoxicity in human carcinoma HEp2 cells. The study concluded that among the conjugates, those bearing an indolyl styryl group (conjugates 4 and 5) showed increased cellular uptake and cytotoxicity. Notably, conjugate 5, which contains a cyclic peptide, demonstrated the highest accumulation in EGFR-overexpressing cells, likely due to its more rigid conformation being more suitable for EGFR binding. Competitive binding studies indicated that conjugate 5 specifically binds to EGFR-overexpressing colon cancer cells, showing potential utility in in vivo imaging applications.
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