Explore a selection of our essential drug information below, or:
Identification
- Generic Name
- Tanespimycin
- DrugBank Accession Number
- DB05134
- Background
Tanespimycin, manufactured by Conforma Therapeutics is under development as a small molecule inhibitor of heat shock protein 90 (HSP90). It is developed for the treatment of several types of cancer, solid tumors or chronic myelogenous leukemia.
- Type
- Small Molecule
- Groups
- Investigational
- Structure
Structure for Tanespimycin (DB05134)
- Weight
- Average: 585.698
Monoisotopic: 585.305015357 - Chemical Formula
- C31H43N3O8
- Synonyms
- 17-allylamino-17-demethoxygeldanamycin
- 17-allylamino-17-demethoxygeldanamycin (17-AGG)
- 17AAG
- Tanespimycin
- tanespimycina
- External IDs
- 17-AAG
- BMS-722782
- CNF-1010
- CNF1010
- KOS-953
Pharmacology
- Indication
Investigated for use/treatment in leukemia (myeloid) and solid tumors.
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Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API- Pharmacodynamics
Not Available
- Mechanism of action
Tanespimycin is a small molecule inhibitor of heat shock protein 90 (HSP90). HSP90 is a molecular “chaperone” protein that controls protein shape or conformation, including that of key signaling molecules involved in the growth and survival of tumor cells.
Target Actions Organism AHeat shock protein HSP 90-alpha inhibitorHumans UHeat shock protein HSP 90-beta 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 macrolactams. These are cyclic amides of amino carboxylic acids, having a 1-azacycloalkan-2-one structure, or analogues having unsaturation or heteroatoms replacing one or more carbon atoms of the ring. They are nitrogen analogues (the a nitrogen atom replacing the o atom of the cyclic carboxylic acid group ) of the naturally occurring macrolides.
- Kingdom
- Organic compounds
- Super Class
- Phenylpropanoids and polyketides
- Class
- Macrolactams
- Sub Class
- Not Available
- Direct Parent
- Macrolactams
- Alternative Parents
- Vinylogous amides / Carbamate esters / Secondary carboxylic acid amides / Secondary alcohols / Organic carbonic acids and derivatives / Lactams / Cyclic ketones / Enamines / Dialkylamines / Dialkyl ethers show 4 more
- Substituents
- Alcohol / Aliphatic heteropolycyclic compound / Amine / Amino acid or derivatives / Azacycle / Carbamic acid ester / Carbonic acid derivative / Carbonyl group / Carboxamide group / Carboxylic acid derivative show 20 more
- Molecular Framework
- Aliphatic heteropolycyclic compounds
- External Descriptors
- secondary amino compound, lactam, macrocycle, benzoquinones (CHEBI:64153)
- Affected organisms
- Not Available
Chemical Identifiers
- UNII
- 4GY0AVT3L4
- CAS number
- 75747-14-7
- InChI Key
- AYUNIORJHRXIBJ-TXHRRWQRSA-N
- InChI
- InChI=1S/C31H43N3O8/c1-8-12-33-26-21-13-17(2)14-25(41-7)27(36)19(4)15-20(5)29(42-31(32)39)24(40-6)11-9-10-18(3)30(38)34-22(28(21)37)16-23(26)35/h8-11,15-17,19,24-25,27,29,33,36H,1,12-14H2,2-7H3,(H2,32,39)(H,34,38)/b11-9-,18-10+,20-15+/t17-,19+,24+,25+,27-,29+/m1/s1
- IUPAC Name
- {[(4E,6Z,8S,9S,10E,12S,13R,14S,16R)-3,13-dihydroxy-8,14-dimethoxy-4,10,12,16-tetramethyl-20,22-dioxo-19-[(prop-2-en-1-yl)amino]-2-azabicyclo[16.3.1]docosa-1(21),2,4,6,10,18-hexaen-9-yl]oxy}methanimidic acid
- SMILES
- [H]/C1=C([H])/[C@]([H])(OC)[C@@]([H])(OC(O)=N)C(C)=C([H])[C@]([H])(C)[C@@]([H])(O)[C@]([H])(C[C@]([H])(C)CC2=C(NCC=C)C(=O)C=C(N=C(O)\C(C)=C\1/[H])C2=O)OC
References
- General References
- Not Available
- External Links
- PubChem Compound
- 6505803
- PubChem Substance
- 347827713
- ChemSpider
- 21106220
- BindingDB
- 50008057
- ChEBI
- 64153
- ChEMBL
- CHEMBL109480
- ZINC
- ZINC000100014666
- Wikipedia
- Tanespimycin
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 data3 Completed Treatment Multiple Myeloma (MM) 1 somestatus stop reason just information to hide 2 Completed Treatment Adenocarcinoma of Prostate / Recurrent Prostate Cancer / Stage IV Prostate Cancer 1 somestatus stop reason just information to hide 2 Completed Treatment Advanced Malignant Neoplasm 1 somestatus stop reason just information to hide 2 Completed Treatment Anaplastic Large Cell Lymphoma / Recurrent Adult Hodgkin's Lymphoma / Recurrent Mantle Cell Lymphoma 1 somestatus stop reason just information to hide 2 Completed Treatment Chronic Myeloproliferative Disorders / Leukemias / Lymphoma / Non Neoplastic Condition / Precancerous Conditions 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
- Not Available
- Predicted Properties
Property Value Source Water Solubility 0.00715 mg/mL ALOGPS logP 2.53 ALOGPS logP 1.52 Chemaxon logS -4.9 ALOGPS pKa (Strongest Acidic) -2.9 Chemaxon pKa (Strongest Basic) 11.59 Chemaxon Physiological Charge 0 Chemaxon Hydrogen Acceptor Count 11 Chemaxon Hydrogen Donor Count 5 Chemaxon Polar Surface Area 170.76 Å2 Chemaxon Rotatable Bond Count 7 Chemaxon Refractivity 175.25 m3·mol-1 Chemaxon Polarizability 61.3 Å3 Chemaxon Number of Rings 2 Chemaxon Bioavailability 0 Chemaxon Rule of Five No Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
- Not Available
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 250.1305485 predictedDarkChem Lite v0.1.0 [M-H]- 242.30763 predictedDeepCCS 1.0 (2019) [M+H]+ 250.2977485 predictedDarkChem Lite v0.1.0 [M+H]+ 244.03136 predictedDeepCCS 1.0 (2019) [M+Na]+ 249.6190485 predictedDarkChem Lite v0.1.0 [M+Na]+ 250.35945 predictedDeepCCS 1.0 (2019)
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Inhibitor
- General Function
- Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812)
- Specific Function
- ATP binding
- Gene Name
- HSP90AA1
- Uniprot ID
- P07900
- Uniprot Name
- Heat shock protein HSP 90-alpha
- Molecular Weight
- 84659.015 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]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059)
- Specific Function
- ATP binding
- Gene Name
- HSP90AB1
- Uniprot ID
- P08238
- Uniprot Name
- Heat shock protein HSP 90-beta
- Molecular Weight
- 83263.475 Da
Carriers
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (PubMed:19021548). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017)
- Specific Function
- antioxidant activity
- Gene Name
- ALB
- Uniprot ID
- P02768
- Uniprot Name
- Albumin
- Molecular Weight
- 69365.94 Da
References
- Guo W, Siegel D, Ross D: Stability of the Hsp90 inhibitor 17AAG hydroquinone and prevention of metal-catalyzed oxidation. J Pharm Sci. 2008 Dec;97(12):5147-57. doi: 10.1002/jps.21394. [Article]
Drug created at October 21, 2007 22:23 / Updated at August 26, 2024 19:23