233272-36-1

Basic information

• Product Name: 1-(7-NITRO-1,2,3,4-TETRAHYDROISOQUINOLIN-3-YL)ETHENOL
• Synonyms: 1-(7-NITRO-1,2,3,4-TETRAHYDROISOQUINOLIN-3-YL)ETHENOL;7-nitro-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid
• CAS NO: 233272-36-1
• Molecular Formula: C10H10N2O4
• Molecular Weight: 222.2
• Mol File: 233272-36-1.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 454.1±45.0 °C(Predicted)
• Appearance: /
• Density: 1.420±0.06 g/cm3(Predicted)
• PKA: 2.01±0.20(Predicted)
• CAS DataBase Reference: 1-(7-NITRO-1,2,3,4-TETRAHYDROISOQUINOLIN-3-YL)ETHENOL(CAS DataBase Reference)
• NIST Chemistry Reference: 1-(7-NITRO-1,2,3,4-TETRAHYDROISOQUINOLIN-3-YL)ETHENOL(233272-36-1)
• EPA Substance Registry System: 1-(7-NITRO-1,2,3,4-TETRAHYDROISOQUINOLIN-3-YL)ETHENOL(233272-36-1)

Safety Data

• Hazardous Substances Data: 233272-36-1(Hazardous Substances Data)

Usage

General Description

1-(7-NITRO-1,2,3,4-TETRAHYDROISOQUINOLIN-3-YL)ETHENOL is a chemical compound with a nitro group attached to a tetrahydroisoquinolin-3-yl moiety and an ethenol group. It is used in pharmaceutical research and drug development as a potential therapeutic agent. The compound has shown promise in preclinical studies for its potential pharmacological properties, including its ability to interact with biological targets and molecular pathways. Its unique structure and chemical properties make it an interesting candidate for further investigation and potential application in the treatment of various diseases and conditions.

Upstream product

• 103733-65-9 (3R)-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid 
• 74163-81-8 L-Tic-OH 

Downstream Products

• 236429-63-3 7-amino-1,2,3,4-tetrahydro-3-isoquinolinecarboxylic acid 

Relevant articles and documents

Design, syntheses, and pharmacological characterization of 17-cyclopropylmethyl-3,14β-dihydroxy-4,5α-epoxy-6α-(isoquinoline-3′-carboxamido)morphinan analogues as opioid receptor ligands

A series of 17-cyclopropylmethyl-3,14β-dihydroxy-4,5α-epoxy-6α-(isoquinoline-3′-carboxamido)morphinan (NAQ) analogues were synthesized and pharmacologically characterized to study their structure-activity relationship at the mu opioid receptor (MOR). The competition binding assay showed two-atom spacer and aromatic side chain were optimal for MOR selectivity. Meanwhile, substitutions at the 1′- and/or 4′-position of the isoquinoline ring retained or improved MOR selectivity over the kappa opioid receptor while still possessing above 20-fold MOR selectivity over the delta opioid receptor. In contrast, substitutions at the 6′- and/or 7′-position of the isoquinoline ring reduced MOR selectivity as well as MOR efficacy. Among this series of ligands, compound 11 acted as an antagonist when challenged with morphine in warm-water tail immersion assay and produced less significant withdrawal symptoms compared to naltrexone in morphine-pelleted mice. Compound 11 also antagonized the intracellular Ca2+ increase induced by DAMGO. Molecular dynamics simulation studies of 11 in three opioid receptors indicated orientation of the 6′-nitro group varied significantly in the different 'address' domains of the receptors and played a crucial role in the observed binding affinities and selectivity. Collectively, the current findings provide valuable insights for future development of NAQ-based MOR selective ligands.

1,2,3,4-Tetrahydroisoquinolinyl sulfamic acids as phosphatase PTP1B inhibitors

High-throughput screening of the P&GP corporate repository against several protein tyrosine phosphatases identified the sulfamic acid moiety as potential phosphotyrosine mimetic. Incorporation of the sulfamic acid onto a 1,2,3,4-tetrahydroisoquinoline sca

Tetrahydroisoquinoline-3-carboxylate based matrix-metalloproteinase inhibitors: Design, synthesis and structure-activity relationship

The design, synthesis and structure-activity relationship (SAR) of a series of nonpeptidic 2-arylsulfonyl-1,2,3,4-tetrahydro-isoquinoline-3-carboxylates and-hydroxamates as inhibitors of the matrix metalloproteinase human neutrophil collagenase (MMP-8) is described here. Based on available X-ray structures of MMP-8/inhibitor complexes, our structure-based design strategy was directed to complement major protein-ligand interaction regions mainly in the S1′ hydrophobic specificity pocket close to the catalytic zinc ion. Here, the rigid 1,2,3,4-tetrahydroisoquinoline scaffold (Tic) provides ideal geometry to combine hydroxamates and carboxylates as typical zinc complexing functionalities, with a broad variety of S1′ directed mono- and biaryl substituents consisting of aromatic rings perfectly accommodated within this more hydrophobic region of the MMP-8 inhibitor binding site. The effect of different S1′ directed substituents, zinc-complexing groups, chirality and variations of the tetrahydroisoquinoline ring-system is investigated by systematic studies. X-ray structure analyses in combination with 3D-QSAR studies provided an additional understanding of key determinants for MMP-8 affinity in this series. The hypothetical binding mode for a typical molecule as basis for our inhibitor design was found in good agreement with a 1.7 A X-ray structure of this candidate in complex with the catalytic domain of human MMP-8. After analysis of all systematic variations, 3D-QSAR and X-ray structure analysis, novel S1′ directed substituents were designed and synthesized and biologically evaluated. This finally results in inhibitors, which do not only show high biological affinity for MMP-8, but also exhibit good oral bioavailability in several animal species.