116027-13-5

Basic information

• Product Name: 3(4H)-Quinazolineacetic acid, 2-chloro-6-iodo-, ethyl ester
• Synonyms: 3(4H)-Quinazolineacetic acid, 2-chloro-6-iodo-, ethyl ester;Ethyl 2-(2-chloro-6-iodoquinazolin-3(4H)-yl)acetate
• CAS NO: 116027-13-5
• Molecular Formula: C₁₂H₁₂ClIN₂O₂
• Molecular Weight: 378.59335
• Mol File: 116027-13-5.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: 2-8°C
• CAS DataBase Reference: 3(4H)-Quinazolineacetic acid, 2-chloro-6-iodo-, ethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: 3(4H)-Quinazolineacetic acid, 2-chloro-6-iodo-, ethyl ester(116027-13-5)
• EPA Substance Registry System: 3(4H)-Quinazolineacetic acid, 2-chloro-6-iodo-, ethyl ester(116027-13-5)

Safety Data

• Hazardous Substances Data: 116027-13-5(Hazardous Substances Data)

Usage

General Description

3(4H)-Quinazolineacetic acid, 2-chloro-6-iodo-, ethyl ester is a chemical compound with the molecular formula C12H11ClIN2O2. It is an ethyl ester derivative of quinazolineacetic acid, and it contains a chlorine atom and an iodine atom in its structure. 3(4H)-Quinazolineacetic acid, 2-chloro-6-iodo-, ethyl ester is commonly used in the field of organic chemistry as a building block for the synthesis of various biologically active molecules and pharmaceuticals. Its unique structure and properties make it a valuable intermediate in the production of new drugs and chemical compounds. Additionally, it has the potential to be used in research and development for pharmaceutical applications due to its biological activity and potential therapeutic properties.

Upstream product

• 16353-27-8 6-Iodo-1H-quinazoline-2,4-dione 
• 116027-11-3 N-<4-iodo-2-(methoxycarbonyl)phenyl>urea 
• 74173-76-5 2,4-dichloro-6-iodoquinazoline 
• 5326-47-6 2-amino-5-iodobenzoic acid 
• 77317-55-6 methyl 2-amino-5-iodobenzoate 
• 116027-10-2 5-iodoisatoic anhydride 
• 105-36-2 ethyl bromoacetate 
• 116027-12-4 2-chloro-6-iodo-3,4-dihydroquinazoline 

Downstream Products

• 108857-18-7 7-iodo-1,2,3,5-tetrahydroimidazo<2,1-b>quinazolin-2(1H)-one 

Relevant articles and documents

Inhibitors of Cyclic AMP Phosphodiesterase. 3. Synthesis and Biological Evaluation of Pyrido and Imidazolyl Analogues of 1,2,3,5-Tetrahydro-2-oxoimidazoquinazoline

Hybridization of structural elements of 1,2,3,5-tetrahydro-2-oxoimidazoquinazoline ring system common to the cyclic AMP (cAMP) phosphodiesterase (PDE) inhibitors lixazinone (RS-82856,1) and anagrelide (3) with complementary features of other PDE inhibitor cardiotonic agents prompted the design and synthesis of the title compounds 7a-d, 11, 12, and 13a,b.The necessary features of these compounds were determined within the framework of the proposed active-site models for the high affinity form of cAMP PDE inhibited by cGMP (type IV).Evaluation of these targets, both in vitro as inhibitors of platelet or cardiac type IV PDE or in vivo as inotropic agents in the pentobarbital-anesthetized dog model of congestive heart failure, showed that these structure possessed negligibly enhanced activities over the parent heterocyclic system, and remained significantly inferior to 1 in all respects.This difference is ascribed to the absence of the N-cyclohexyl-N-methylbutyramidyl-4-oxy side chain of 1.The proposal that the acidic lactam-type functionality, common to the type IV PDE inhibitor inotropic agents such as 4-6 and 8-10, mimics the polarizable cyclic phosphate moiety of cAMP suggested that the side chain of 1 may function as an effective surrogate for selected characteristics of the adenine portion of cAMP.However, the results of this study show that incorporation of adenine-like hydrogen-bonding functionalities common to other type IV PDE inhibitors into the 1,2,3,5-tetrahydro-2-oxoimidazoquinazoline system did not enhance activity to the levels observed for 1 analogues.These observations, coupled with the kinetic pattern of inhibition of type IV PDE observed for 1 and analogues, suggest that access to a secondary, lipophilic-tolerant binding site, possibly coincident with the adenine binding domain, and adjacent to the catalytic ribose-phosphate binding site of platelet and cardiac type IV PDE, is responsible for the increased potency of these compounds.