Sphingosine
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Identification
- Generic Name
- Sphingosine
- DrugBank Accession Number
- DB03203
- Background
An amino alcohol with a long unsaturated hydrocarbon chain. Sphingosine and its derivative sphinganine are the major bases of the sphingolipids in mammals. (Dorland, 28th ed)
- Type
- Small Molecule
- Groups
- Experimental
- Structure
- Weight
- Average: 299.4919
Monoisotopic: 299.282429433 - Chemical Formula
- C18H37NO2
- Synonyms
- Not Available
Pharmacology
- Indication
Not Available
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- Pharmacodynamics
Not Available
- Mechanism of action
Target Actions Organism ACholine-phosphate cytidylyltransferase B inhibitorHumans UGenome polyprotein Not Available Poliovirus type 1 (strain Mahoney) UGenome polyprotein Not Available HRV-14 UGenome polyprotein Not Available SVDV UGenome polyprotein Not Available Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B) UPoliovirus receptor Not Available Humans UGlycolipid transfer protein Not Available Humans - Absorption
Not Available
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
Not Available
- Clearance
Not Available
- Adverse Effects
- Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.
- Toxicity
Not Available
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.Not Available
- Food Interactions
- Not Available
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as 1,2-aminoalcohols. These are organic compounds containing an alkyl chain with an amine group bound to the C1 atom and an alcohol group bound to the C2 atom.
- Kingdom
- Organic compounds
- Super Class
- Organic nitrogen compounds
- Class
- Organonitrogen compounds
- Sub Class
- Amines
- Direct Parent
- 1,2-aminoalcohols
- Alternative Parents
- Secondary alcohols / Primary alcohols / Organopnictogen compounds / Monoalkylamines / Hydrocarbon derivatives
- Substituents
- 1,2-aminoalcohol / Alcohol / Aliphatic acyclic compound / Hydrocarbon derivative / Organic oxygen compound / Organooxygen compound / Organopnictogen compound / Primary alcohol / Primary aliphatic amine / Primary amine
- Molecular Framework
- Aliphatic acyclic compounds
- External Descriptors
- sphing-4-enine (CHEBI:16393) / Sphing-4-enines (Sphingosines) (C00319) / Sphing-4-enines (Sphingosines) (LMSP01010001)
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- NGZ37HRE42
- CAS number
- 123-78-4
- InChI Key
- WWUZIQQURGPMPG-KRWOKUGFSA-N
- InChI
- InChI=1S/C18H37NO2/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-18(21)17(19)16-20/h14-15,17-18,20-21H,2-13,16,19H2,1H3/b15-14+/t17-,18+/m0/s1
- IUPAC Name
- (2S,3R,4E)-2-aminooctadec-4-ene-1,3-diol
- SMILES
- [H]\C(CCCCCCCCCCCCC)=C(\[H])[C@@]([H])(O)[C@@]([H])(N)CO
References
- Synthesis Reference
Dennis Liotta, Alfred H. Merrill, "Method of preparing sphingosine derivatives." U.S. Patent US5110987, issued August, 1976.
US5110987- General References
- Not Available
- External Links
- KEGG Compound
- C00319
- PubChem Compound
- 5280335
- PubChem Substance
- 46505156
- ChemSpider
- 4444047
- BindingDB
- 83205
- ChEBI
- 16393
- ChEMBL
- CHEMBL67166
- ZINC
- ZINC000008195650
- Therapeutic Targets Database
- DNC001357
- Guide to Pharmacology
- GtP Drug Page
- PDBe Ligand
- SQS
- Wikipedia
- Sphingosine
- PDB Entries
- 3vzb / 8c6d
Clinical Trials
- Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample dataNot Available Recruiting Not Available Alzheimer's Disease (AD) 1 somestatus stop reason just information to hide 1 Completed Treatment Pancreatic Cancer / Unspecified Adult Solid Tumor, Protocol Specific 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
- Not Available
- Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 67 °C PhysProp - Predicted Properties
Property Value Source Water Solubility 0.0039 mg/mL ALOGPS logP 5.15 ALOGPS logP 4.57 Chemaxon logS -4.9 ALOGPS pKa (Strongest Acidic) 14.12 Chemaxon pKa (Strongest Basic) 9.23 Chemaxon Physiological Charge 1 Chemaxon Hydrogen Acceptor Count 3 Chemaxon Hydrogen Donor Count 3 Chemaxon Polar Surface Area 66.48 Å2 Chemaxon Rotatable Bond Count 15 Chemaxon Refractivity 91.89 m3·mol-1 Chemaxon Polarizability 39.37 Å3 Chemaxon Number of Rings 0 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter Yes Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
Property Value Probability Human Intestinal Absorption + 0.995 Blood Brain Barrier + 0.5839 Caco-2 permeable - 0.573 P-glycoprotein substrate Substrate 0.5295 P-glycoprotein inhibitor I Non-inhibitor 0.9155 P-glycoprotein inhibitor II Non-inhibitor 0.7564 Renal organic cation transporter Non-inhibitor 0.8759 CYP450 2C9 substrate Non-substrate 0.8247 CYP450 2D6 substrate Non-substrate 0.706 CYP450 3A4 substrate Non-substrate 0.7191 CYP450 1A2 substrate Inhibitor 0.9106 CYP450 2C9 inhibitor Non-inhibitor 0.9071 CYP450 2D6 inhibitor Inhibitor 0.8932 CYP450 2C19 inhibitor Non-inhibitor 0.9025 CYP450 3A4 inhibitor Non-inhibitor 0.9151 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.7332 Ames test Non AMES toxic 0.7957 Carcinogenicity Non-carcinogens 0.7754 Biodegradation Ready biodegradable 0.748 Rat acute toxicity 1.6142 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.8822 hERG inhibition (predictor II) Non-inhibitor 0.854
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 209.9425712 predictedDarkChem Lite v0.1.0 [M-H]- 185.61954 predictedDeepCCS 1.0 (2019) [M+H]+ 209.9055712 predictedDarkChem Lite v0.1.0 [M+H]+ 188.53503 predictedDeepCCS 1.0 (2019) [M+Na]+ 208.9045712 predictedDarkChem Lite v0.1.0 [M+Na]+ 196.28209 predictedDeepCCS 1.0 (2019)
Targets
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1. DetailsCholine-phosphate cytidylyltransferase B
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis
- Specific Function
- choline-phosphate cytidylyltransferase activity
- Gene Name
- PCYT1B
- Uniprot ID
- Q9Y5K3
- Uniprot Name
- Choline-phosphate cytidylyltransferase B
- Molecular Weight
- 41939.76 Da
References
- Zhou Y, Zhang Y, Zhao D, Yu X, Shen X, Zhou Y, Wang S, Qiu Y, Chen Y, Zhu F: TTD: Therapeutic Target Database describing target druggability information. Nucleic Acids Res. 2024 Jan 5;52(D1):D1465-D1477. doi: 10.1093/nar/gkad751. [Article]
2. DetailsGenome polyprotein
- Kind
- Protein
- Organism
- Poliovirus type 1 (strain Mahoney)
- Pharmacological action
- Unknown
- General Function
- Capsid protein VP1 Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:2994218). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (PubMed:2994218). Capsid protein VP1 mainly forms the vertices of the capsid (PubMed:23365424). Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host epithelial cells (PubMed:25631086). This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells (PubMed:17622193, PubMed:17717529, PubMed:18191571). Tyrosine kinases are probably involved in the entry process (PubMed:17717529). Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins (PubMed:17717529). Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS (PubMed:17717529). After binding to its receptor, the capsid undergoes conformational changes (PubMed:25631086). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (PubMed:25631086). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (PubMed:25631086).
- Specific Function
- ATP binding
- Gene Name
- Not Available
- Uniprot ID
- P03300
- Uniprot Name
- Genome polyprotein
- Molecular Weight
- 246538.14 Da
References
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
3. DetailsGenome polyprotein
- Kind
- Protein
- Organism
- HRV-14
- Pharmacological action
- Unknown
- General Function
- Capsid protein VP1 Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host ICAM1 to provide virion attachment to target host cells (PubMed:10562537). This attachment induces virion internalization (By similarity). Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (Probable). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (PubMed:28696310). After genome has been released, the channel shrinks.
- Specific Function
- ATP binding
- Gene Name
- Not Available
- Uniprot ID
- P03303
- Uniprot Name
- Genome polyprotein
- Molecular Weight
- 242989.38 Da
References
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
4. DetailsGenome polyprotein
- Kind
- Protein
- Organism
- SVDV
- Pharmacological action
- Unknown
- General Function
- Capsid protein VP1 Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1 interacts with host CXADR to provide virion attachment to target host cells (Probable). This attachment induces virion internalization (By similarity). Tyrosine kinases are probably involved in the entry process (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity).
- Specific Function
- ATP binding
- Gene Name
- Not Available
- Uniprot ID
- P13900
- Uniprot Name
- Genome polyprotein
- Molecular Weight
- 243363.48 Da
References
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
5. DetailsGenome polyprotein
- Kind
- Protein
- Organism
- Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B)
- Pharmacological action
- Unknown
- General Function
- Capsid protein VP1 Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells (By similarity). Tyrosine kinases are probably involved in the entry process (By similarity). Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins (By similarity). Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity).
- Specific Function
- ATP binding
- Gene Name
- Not Available
- Uniprot ID
- P03302
- Uniprot Name
- Genome polyprotein
- Molecular Weight
- 246162.675 Da
References
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
6. DetailsPoliovirus receptor
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration
- Specific Function
- cell adhesion molecule binding
- Gene Name
- PVR
- Uniprot ID
- P15151
- Uniprot Name
- Poliovirus receptor
- Molecular Weight
- 45302.3 Da
References
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
7. DetailsGlycolipid transfer protein
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides
- Specific Function
- ceramide 1-phosphate binding
- Gene Name
- GLTP
- Uniprot ID
- Q9NZD2
- Uniprot Name
- Glycolipid transfer protein
- Molecular Weight
- 23849.6 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
Transporters
1. DetailsATP-dependent translocase ABCB1
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Translocates drugs and phospholipids across the membrane (PubMed:2897240, PubMed:35970996, PubMed:8898203, PubMed:9038218). Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins (PubMed:8898203). Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells (PubMed:2897240, PubMed:35970996, PubMed:9038218)
- Specific Function
- ABC-type xenobiotic transporter activity
- Gene Name
- ABCB1
- Uniprot ID
- P08183
- Uniprot Name
- ATP-dependent translocase ABCB1
- Molecular Weight
- 141477.255 Da
References
- Sugawara T, Kinoshita M, Ohnishi M, Tsuzuki T, Miyazawa T, Nagata J, Hirata T, Saito M: Efflux of sphingoid bases by P-glycoprotein in human intestinal Caco-2 cells. Biosci Biotechnol Biochem. 2004 Dec;68(12):2541-6. [Article]
Drug created at June 13, 2005 13:24 / Updated at August 26, 2024 19:24