90800-31-0

Basic information

• Product Name: 2-HYDROXYQUINOLINE-6-CARBALDEHYDE
• Synonyms: 2-HYDROXYQUINOLINE-6-CARBALDEHYDE;2-Hydroxy-6-quinolinecarboxaldehyde;2-Oxo-1,2-dihydro-6-quinolinecarboxaldehyde;1,2-dihydro-2-oxo-6-quinolinecarboxaldehyde
• CAS NO: 90800-31-0
• Molecular Formula: C10H7NO2
• Molecular Weight: 173.16808
• Mol File: 90800-31-0.mol
• Article Data: 4

Chemical Properties

• Melting Point: 284-285.5℃
• Appearance: /
• CAS DataBase Reference: 2-HYDROXYQUINOLINE-6-CARBALDEHYDE(CAS DataBase Reference)
• NIST Chemistry Reference: 2-HYDROXYQUINOLINE-6-CARBALDEHYDE(90800-31-0)
• EPA Substance Registry System: 2-HYDROXYQUINOLINE-6-CARBALDEHYDE(90800-31-0)

Safety Data

• Hazardous Substances Data: 90800-31-0(Hazardous Substances Data)

Upstream product

• 103702-41-6 6-(1-hydroxy-2-isopropylaminopropyl)-2-(1H)-quinolinone 
• 791626-62-5 2-chloro-6-(1,3-dioxolan-2-yl)quinoline 
• 4295-11-8 2-chloro-6-methylquinoline 
• 791626-59-0 2-chloroquinoline-6-carbaldehyde 

Downstream Products

• 103702-29-0 6-Bromomethyl-1H-quinolin-2-one 

Relevant articles and documents

NEW BICYCLIC DERIVATIVES HAVING BETA2 ADRENERGIC AGONIST AND M3 MUSCARINIC ANTAGONIST ACTIVITIES

The present invention relates to novel compounds having β2 adrenergic agonist and M3 muscarinic antagonist dual activity, to pharmaceutical compositions containing them, to the process for their preparation and to their use in respiratory therapies.

Identification and specificity studies of small-molecule ligands for SH3 protein domains

The Src Homology 3 (SH3) domains are small protein-protein interaction domains that bind proline-rich sequences and mediate a wide range of cell-signaling and other important biological processes. Since deregulated signaling pathways form the basis of many human diseases, the SH3 domains have been attractive targets for novel therapeutics. High-affinity ligands for SH3 domains have been designed; however, these have all been peptide-based and no examples of entirely nonpeptide SH3 ligands have previously been reported. Using the mouse Tec Kinase SH3 domain as a model system for structure-based ligand design, we have identified several simple heterocyclic compounds that selectively bind to the Tec SH3 domain. Using a combination of nuclear magnetic resonance chemical shift perturbation, structure-activity relationships, and site-directed mutagenesis, the binding of these compounds at the proline-rich peptide-binding site has been characterized. The most potent of these, 2-aminoquinoline, bound with Kd = 125 μM and was able to compete for binding with a proline-rich peptide. Synthesis of 6-substitued-2- aminoquinolines resulted in ligands with up to 6-fold improved affinity over 2-aminoquinoline and enhanced specificity for the Tec SH3 domain. Therefore, 2-aminoquinolines may potentially be useful for the development of high affinity small molecule ligands for SH3 domains.