54810-63-8

Basic information

• Product Name: Methyl 2-Chloro-5-methoxybenzoate
• Synonyms: Methyl 2-Chloro-5-methoxybenzoate
• CAS NO: 54810-63-8
• Molecular Formula: C₉H₉ClO₃
• Molecular Weight: 200.61896
• Mol File: 54810-63-8.mol
• Article Data: 8

Chemical Properties

• Boiling Point: 108-110 °C(Press: 0.2 Torr)
• Appearance: /
• Density: 1.228±0.06 g/cm3(Predicted)
• Storage Temp.: Sealed in dry,Room Temperature
• CAS DataBase Reference: Methyl 2-Chloro-5-methoxybenzoate(CAS DataBase Reference)
• NIST Chemistry Reference: Methyl 2-Chloro-5-methoxybenzoate(54810-63-8)
• EPA Substance Registry System: Methyl 2-Chloro-5-methoxybenzoate(54810-63-8)

Safety Data

• Hazardous Substances Data: 54810-63-8(Hazardous Substances Data)

Usage

General Description

Methyl 2-Chloro-5-methoxybenzoate is a chemical compound with the molecular formula C9H9ClO3. It is a derivative of benzoic acid, with a methyl group and a methoxy group attached to the benzene ring, as well as a chlorine atom in the para position. Methyl 2-Chloro-5-methoxybenzoate is commonly used as an intermediate in the synthesis of pharmaceuticals and agrochemicals, as well as in the production of fragrances and flavors. It is a white to light yellow crystalline solid with a characteristic odor and is mainly used in the manufacturing of various products in the chemical industry.

InChI:InChI=1/C9H9ClO3/c1-12-6-3-4-8(10)7(5-6)9(11)13-2/h3-5H,1-2H3

Upstream product

• 67-56-1 methanol 
• 586-38-9 3-Methoxybenzoic acid 
• 6280-89-3 2-chloro-5-methoxybenzoic acid 
• 56961-30-9 2-chloro-5-hydroxybenzoic acid 
• 74-88-4 methyl iodide 
• 5368-81-0 methyl 3-methoxybenzoate 
• 89-54-3 2-chloro-5-aminobenzoic acid 

Downstream Products

• 56961-30-9 2-chloro-5-hydroxybenzoic acid 
• 882674-30-8 2-(2-chloro-5-methoxyphenyl)ethan-1-amine 
• 13719-61-4 2-chloro-5-methoxybenzaldehyde 
• 1417409-64-3 8-bromo-1-(2-chloro-5-methoxyphenyl)-4-methyl[1,2,4]triazolo[4,3-a]quinoxaline 
• 1417409-83-6 1-(2-chloro-5-methoxyphenyl)-4-methyl-8-(morpholin-4-ylmethyl)[1,2,4]triazolo[4,3-a]quinoxaline 
• 92492-22-3 4-(2-Chlor-5-methoxy-phenyl)-buttersaeure 
• 90919-41-8 (2-chloro-5-methoxy-phenyl)-acetic acid methyl ester 
• 90562-49-5 C-(2-Chlor-5-methoxy-phenyl)-acetamid 
• 93089-30-6 2-<β-(2-Chlor-5-methoxy-phenyl)-ethyl>-malonsaeure-diethylester 
• 91393-84-9 2-<β-(2-Chlor-5-methoxy-phenyl)-ethyl>-malonsaeure 
• 91367-10-1 2-(2-chloro-5-methoxy-phenyl)acetic acid 

Relevant articles and documents

ADAMANTANYL-SUBSTITUTED BENZAMIDE COMPOUNDS AND THEIR USE AS P2X7 RECEPTOR ANTAGONISTS

The present invention relates to adamantanyl-substituted benzamide compounds and their use as antagonists of the P2X7 purinoreceptor. The invention further relates to methods for the treatment of disease and conditions associated with the P2X7 purinoreceptor.

Optimization of a Benzoylpiperidine Class Identifies a Highly Potent and Selective Reversible Monoacylglycerol Lipase (MAGL) Inhibitor

Monoacylglycerol lipase (MAGL) is the enzyme degrading the endocannabinoid 2-arachidonoylglycerol, and it is involved in several physiological and pathological processes. The therapeutic potential of MAGL is linked to several diseases, including cancer. The development of MAGL inhibitors has been greatly limited by the side effects associated with the prolonged MAGL inactivation. Importantly, it could be preferable to use reversible MAGL inhibitors in vivo, but nowadays only few reversible compounds have been developed. In the present study, structural optimization of a previously developed class of MAGL inhibitors led to the identification of compound 23, which proved to be a very potent reversible MAGL inhibitor (IC50 = 80 nM), selective for MAGL over the other main components of the endocannabinoid system, endowed of a promising antiproliferative activity in a series of cancer cell lines and able to block MAGL both in cell-based as well as in vivo assays.

Mathematical and Structural Characterization of Strong Nonadditive Structure-Activity Relationship Caused by Protein Conformational Changes

In medicinal chemistry, accurate prediction of additivity-based structure-activity relationship (SAR) analysis rests on three assumptions: (1) a consistent binding pose of the central scaffold, (2) no interaction between the R group substituents, and (3) a relatively rigid binding pocket in which the R group substituents act independently. Previously, examples of nonadditive SAR have been documented in systems that deviate from the first two assumptions. Local protein structural change upon ligand binding, through induced fit or conformational selection, although a well-known phenomenon that invalidates the third assumption, has not been linked to nonadditive SAR conclusively. Here, for the first time, we present clear structural evidence that the formation of a hydrophobic pocket upon ligand binding in PDE2 catalytic site reduces the size of another distinct subpocket and contributes to strong nonadditive SAR between two otherwise distant R groups.