191326-92-8

Basic information

• Product Name: 3-Isoquinolinecarboxylic acid, 2-([1,1'-biphenyl]-4-ylsulfonyl)-1,2,3,4-tetrahydro-, (3R)-
• CAS NO: 191326-92-8
• Molecular Formula: C22H19NO4S
• Molecular Weight: 393.463
• Mol File: 191326-92-8.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: 3-Isoquinolinecarboxylic acid, 2-([1,1'-biphenyl]-4-ylsulfonyl)-1,2,3,4-tetrahydro-, (3R)-(CAS DataBase Reference)
• NIST Chemistry Reference: 3-Isoquinolinecarboxylic acid, 2-([1,1'-biphenyl]-4-ylsulfonyl)-1,2,3,4-tetrahydro-, (3R)-(191326-92-8)
• EPA Substance Registry System: 3-Isoquinolinecarboxylic acid, 2-([1,1'-biphenyl]-4-ylsulfonyl)-1,2,3,4-tetrahydro-, (3R)-(191326-92-8)

Safety Data

• Hazardous Substances Data: 191326-92-8(Hazardous Substances Data)

Upstream product

• 1623-93-4 4-diphenylsulfonyl chloride 
• 103733-65-9 (3R)-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid 
• 7440-44-0 pyrographite 

Downstream Products

• 217300-61-3 C₂₃H₂₂N₂O₃S 
• 217300-60-2 2-(Biphenyl-4-sulfonyl)-1,2,3,4-tetrahydro-isoquinoline-3-carbaldehyde 

Relevant articles and documents

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.

Relative configuration and conformation of key intermediates for matrix metalloproteinase inhibitors as determined by NMR-based restrained simulated annealing and validated by X-ray analysis [2]

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