1254328-26-1

Basic information

• Product Name: Methyl 2,3-dimethylisonicotinate
• Synonyms: Methyl 2,3-dimethylisonicotinate;2,3-Dimethyl-isonicotinic acid methyl ester
• CAS NO: 1254328-26-1
• Molecular Formula: C9H11NO2
• Molecular Weight: 165.192
• Mol File: 1254328-26-1.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: Methyl 2,3-dimethylisonicotinate(CAS DataBase Reference)
• NIST Chemistry Reference: Methyl 2,3-dimethylisonicotinate(1254328-26-1)
• EPA Substance Registry System: Methyl 2,3-dimethylisonicotinate(1254328-26-1)

Safety Data

• Hazardous Substances Data: 1254328-26-1(Hazardous Substances Data)

Usage

General Description

Methyl 2,3-dimethylisonicotinate is a chemical compound with the molecular formula C10H13NO2. It is a derivative of isonicotinic acid and has two methyl groups attached to the 2 and 3 positions of the aromatic ring. Methyl 2,3-dimethylisonicotinate is commonly used as an intermediate in the synthesis of pharmaceuticals and agrochemicals. It is also known for its potential as a ligand in coordination chemistry and as a building block in organic synthesis. Methyl 2,3-dimethylisonicotinate is a yellow-brown solid at room temperature and is sparingly soluble in water. It is important to handle this chemical with care and follow proper safety precautions when working with it in a laboratory setting.

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Relevant articles and documents

Aminopyrazine inhibitors binding to an unusual inactive conformation of the mitotic kinase Nek2: SAR and structural characterization

We report herein the first systematic exploration of inhibitors of the mitotic kinase Nek2. Starting from HTS hit aminopyrazine 2, compounds with improved activity were identified using structure-based design. Our structural biology investigations reveal two notable observations. First, 2 and related compounds bind to an unusual, inactive conformation of the kinase which to the best of our knowledge has not been reported for other types of kinase inhibitors. Second, a phenylalanine residue at the center of the ATP pocket strongly affects the ability of the inhibitor to bind to the protein. The implications of these observations are discussed, and the work described here defines key features for potent and selective Nek2 inhibition, which will aid the identification of more advanced inhibitors of Nek2.