134355-54-7

Basic information

• Product Name: RaceAnisodamine
• Synonyms: RaceAnisodamine
• CAS NO: 134355-54-7
• Molecular Formula: C₁₇H₂₃NO₄
• Molecular Weight: 341.833
• Mol File: 134355-54-7.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 474.6±45.0 °C(Predicted)
• Appearance: White powder
• Density: 1.27±0.1 g/cm3(Predicted)
• Storage Temp.: 2-8°C
• PKA: 14.12±0.10(Predicted)
• CAS DataBase Reference: RaceAnisodamine(CAS DataBase Reference)
• NIST Chemistry Reference: RaceAnisodamine(134355-54-7)
• EPA Substance Registry System: RaceAnisodamine(134355-54-7)

Safety Data

• Hazardous Substances Data: 134355-54-7(Hazardous Substances Data)

Usage

General Description

Raceanisodamine is a chemical compound that belongs to the class of quinuclidine derivatives. It is a cholinergic antagonist used as an antispasmodic and vasodilator. The compound works by blocking the activity of acetylcholine at muscarinic receptors, leading to smooth muscle relaxation and increased blood flow. Raceanisodamine is commonly used to treat gastrointestinal and genitourinary spasms, as well as peripheral arterial disorders. It is available in various formulations including tablets, injectables, and eye drops, and is generally well-tolerated with minimal side effects.

Upstream product

• 32634-68-7 (2S,3S)-di-4-toluoyltartaric acid 
• 101-31-5 Hyoscyamine 
• 1083169-27-0 C₁₅H₂₉NO₄Si 
• 4277-63-8 methyl 1H-pyrrole-1-carboxylate 
• 1001339-25-8 C₁₅H₂₇NO₃Si 
• 6415-90-3 (-)-hyoscyamine hydrobromide 
• 51-34-3 scopolamine 

Downstream Products

• 4839-11-6 (3R,6R)-tropane-3α,6β-diol 
• 51-34-3 scopolamine 
• 16202-15-6 (S)-tropic acid 
• 126211-14-1 3α,6β-dihydroxytropane HCl 

Related news

Mn-doped ZnS quantum dots for the room-temperature phosphorescence detection of RaceAnisodamine (cas 134355-54-7) hydrochloride and atropine sulfate in biological fluids07/25/2019

Now, the development of quantum dots (QDs)-based fluorescence sensors become very quickly, but as phosphorescence compared to fluorescent has many advantages, like longer shine time and emission wavelength. Therefore, the phosphorescence properties of QDs and their potential for phosphorescence ...detailed

Relevant articles and documents

Evidence for Modulation of Oxygen Rebound Rate in Control of Outcome by Iron(II)- And 2-Oxoglutarate-Dependent Oxygenases

Iron(II)- and 2-oxoglutarate-dependent (Fe/2OG) oxygenases generate iron(IV)-oxo (ferryl) intermediates that can abstract hydrogen from aliphatic carbons (R-H). Hydroxylation proceeds by coupling of the resultant substrate radical (Ra€￠) and oxygen of the Fe(III)-OH complex ("oxygen rebound"). Nonhydroxylation outcomes result from different fates of the Fe(III)-OH/R?state; for example, halogenation results from R?coupling to a halogen ligand cis to the hydroxide. We previously suggested that halogenases control substrate-cofactor disposition to disfavor oxygen rebound and permit halogen coupling to prevail. Here, we explored the general implication that, when a ferryl intermediate can ambiguously target two substrate carbons for different outcomes, rebound to the site capable of the alternative outcome should be slower than to the adjacent, solely hydroxylated site. We evaluated this prediction for (i) the halogenase SyrB2, which exclusively hydroxylates C5 of norvaline appended to its carrier protein but can either chlorinate or hydroxylate C4 and (ii) two bifunctional enzymes that normally hydroxylate one carbon before coupling that oxygen to a second carbon (producing an oxacycle) but can, upon encountering deuterium at the first site, hydroxylate the second site instead. In all three cases, substrate hydroxylation incorporates a greater fraction of solvent-derived oxygen at the site that can also undergo the alternative outcome than at the other site, most likely reflecting an increased exchange of the initially O2-derived oxygen ligand in the longer-lived Fe(III)-OH/R?states. Suppression of rebound may thus be generally important for nonhydroxylation outcomes by these enzymes.

Preparative separation of four isomers of synthetic anisodamine by HPLC and diastereomer crystallization

Anisodamine (654-1), a well-known cholinergic antagonist, is marketed as synthetic anisodamine (mixture of four isomers, 654-2) in China. To preparative resolution and comparison of the bioactivities of the four isomers of synthetic anisodamine, current work explores an economic and effective separation method by using preparative high performance liquid chromatography (HPLC) and diastereomer crystallization. Their absolute configurations were established by single-crystal X-ray diffraction and circular dichroism method. The purities of each isomer were more than 95%. Among them, 654-2-A2 (6R, 2′S configuration) exhibited better effect on cabachol preconditioned small intestine tension more than 654-2 and other isomers. The direct separation method without using HPLC was tried as well, which was still on progress. This is the first report of the method for preparative separation of four isomers of synthetic anisodamine which could be used for large-scale production in industry.

Molecular cloning, expression and characterization of hyoscyamine 6β-hydroxylase from hairy roots of Anisodus tanguticus

Anisodus tanguticus, one of the indigenous Chinese ethnological medicinal plants of the Solanaceae, produces anticholinergic alkaloids such as hyoscyamine, 6β-hydroxyhyoscyamine and scopolamine. Hyoscyamine 6β-hydroxylase (H6H), a key enzyme in the biosynthetic pathway of scopolamine, catalyzes the hydroxylation of hyoscyamine and epoxide formation from 6β-hydroxyhyoscyamine to generate scopolamine. A full-length cDNA of H6H has been isolated from A. tanguticus hairy roots. Nucleotide sequence analysis of the cloned cDNA revealed an open reading frame of 1035 bp encoding 344 amino acids with high homology to other known H6Hs. The equivalent amino acid sequence shows a typical motif of 2-oxoglutarate-dependent dioxygenase. The A. tanguticus H6H was expressed in Escherichia coli and purified for enzyme function analysis. This study characterized the recombinant AtH6H and showed it could generate scopolamine from hyoscyamine.