Investigational Drug Details
| Drug ID: | D011 |
| Drug Name: | Ascorbic acid |
| Synonyms: | |
| Type: | small molecule |
| DrugBank ID: | DB00126 |
| DrugBank Description: | A six carbon compound related to glucose. It is found naturally in citrus fruits and many vegetables. Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. Its biologically active form, vitamin C, functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant. |
| PubChem ID: | 54670067 |
| CasNo: | 50-81-7 |
| Repositioning for NAFLD: | Yes |
| SMILES: | [H][C@@]1(OC(=O)C(O)=C1O)[C@@H](O)CO |
| Structure: |
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| InChiKey: | CIWBSHSKHKDKBQ-JLAZNSOCSA-N |
| Molecular Weight: | 176.1241 |
| DrugBank Targets: | Hyaluronate lyase; DNA; Xylose isomerase; Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2; Phytanoyl-CoA dioxygenase, peroxisomal; Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3; Gamma-butyrobetaine dioxygenase; Dopamine beta-hydroxylase; Peptidyl-glycine alpha-amidating monooxygenase; Prolyl 3-hydroxylase 1; Prolyl 3-hydroxylase 2; Prolyl 3-hydroxylase 3; Prolyl 4-hydroxylase subunit alpha-1; 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1; 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2; Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2; Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3; Lysine-specific demethylase 5D; Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1; Trimethyllysine dioxygenase, mitochondrial; Transmembrane prolyl 4-hydroxylase; Egl nine homolog 1; Egl nine homolog 2; Egl nine homolog 3 |
| DrugBank MoA: | In humans, an exogenous source of ascorbic acid is required for collagen formation and tissue repair by acting as a cofactor in the posttranslational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. Ascorbic acid is reversibly oxidized to dehydroascorbic acid in the body. These two forms of the vitamin are believed to be important in oxidation-reduction reactions. The vitamin is involved in tyrosine metabolism, conversion of folic acid to folinic acid, carbohydrate metabolism, synthesis of lipids and proteins, iron metabolism, resistance to infections, and cellular respiration. |
| DrugBank Pharmacology: | Ascorbic Acid (vitamin C) is a water-soluble vitamin indicated for the prevention and treatment of scurvy, as ascorbic acid deficiency results in scurvy. Collagenous structures are primarily affected, and lesions develop in bones and blood vessels. Administration of ascorbic acid completely reverses the symptoms of ascorbic acid deficiency. |
| DrugBank Indication: | Used to treat vitamin C deficiency, scurvy, delayed wound and bone healing, urine acidification, and in general as an antioxidant. It has also been suggested to be an effective antiviral agent. |
| Targets: | |
| Therapeutic Category: | |
| Clinical Trial Progress: | |
| Latest Progress: |
| Trial ID | Source ID | Phases | Status | Study Results | Start Date | Last Update Posted | |
|---|---|---|---|---|---|---|---|
| L0525 | NCT05900635 | PHASE4 | UNKNOWN | NO | 2022-10-01 | 2023-06-12 | Details |
| L1260 | NCT04575896 | PHASE4 | COMPLETED | YES | 2020-11-20 | 2024-01-10 | Details |
| L1457 | NCT04984226 | PHASE2 | RECRUITING | NO | 2023-09-08 | 2024-07-08 | Details |
| L3604 | NCT01923181 | PHASE2 | COMPLETED | YES | 2013-12-02 | 2021-01-15 | Details |
| L5464 | NCT01588470 | PHASE4 | COMPLETED | YES | 2006-06 | 2017-12-06 | Details |
| Target ID | Target Name | GENE | Action | Class | UniProtKB ID | Entry Name | |
|---|---|---|---|---|---|---|---|
| T03 | Angiotensin-converting enzyme | ACE | INHIBITOR | Target is a single protein chain | P12821 | ACE_HUMAN | Details |
| T06 | Sulfonylurea receptor 1 | ABCC8 | Target is a single protein chain | Q09428 | ABCC8_HUMAN | Details | |
| T47 | Sialin | SLC17A5 | Target is a single protein chain | Q9NRA2 | SLC17A5_HUMAN | Details |
| Strategy ID | Strategy | Synonyms | Related Targets | Related Drugs |
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| Article ID | PMID | Source | Title |
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