236403-25-1

Usage

Uses

Used in Pharmaceutical Industry:
MMP-8 INHIBITOR I is used as a therapeutic agent for the treatment of various diseases associated with MMP-8 activity. The primary application is in the inhibition of MMP-8, which can help in managing conditions like atherosclerosis, angiogenesis-related disorders, and potentially aggressive breast cancer.
Used in Research Applications:
MMP-8 INHIBITOR I serves as a valuable research tool for studying the role of MMP-8 in various biological processes and disease mechanisms. It can be used to investigate the effects of MMP-8 inhibition on endothelial cell function, atherosclerotic plaque development, and the mobilization of stem cells.
Used in Drug Development:
MMP-8 INHIBITOR I can be utilized in the development of novel drugs targeting MMP-8 for the treatment of diseases where MMP-8 plays a significant role. This includes the development of more potent and selective inhibitors, as well as combination therapies with other drugs to enhance efficacy and reduce side effects.
Used in Diagnostic Applications:
MMP-8 INHIBITOR I can be employed in the development of diagnostic tools to assess the activity of MMP-8 in patient samples. This can help in the identification of individuals at risk for diseases associated with MMP-8 dysregulation and guide personalized treatment strategies.

Upstream product

• 673-06-3 D-(R)-phenylalanine 
• 98-68-0 4-methoxy-phenyl-sulphonyl chloride 
• 171859-74-8 N-Fmoc-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid 
• 103733-65-9 (3R)-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid 
• 74163-81-8 L-Tic-OH 

Relevant academic research and scientific papers

Characterization of a selective inhibitor for matrix metalloproteinase-8 (MMP-8)

MMP-8 has been implicated in various diseases. Selective MMP-8 inhibitors are needed to ascertain the role of this enzyme. We synthesized two inhibitors reported previously as selective for MMP-8. Compound 1 selectively inhibited MMP-8 and MMP-13; compoun

Preparation of hydroxamic acids from esters in solution and on the solid phase

The present invention provides a novel method for the formation of hydroxamic acids comprising reacting under suitable conditions an ester with hydroxylamine in the presence of cyanide anion.

Improved solution- and solid-phase preparation of hydroxamic acids from esters

The addition of small amounts of solid KCN to solution and solid-phase esters in THF/MeOH/50% aqueous NH2OH increases the efficiency of their transformation to the corresponding hydroxamic acids.

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.