95907-05-4

Usage

Uses

Used in Pharmaceutical Synthesis:
2-Pyridinol,3-methoxy-(9CI) is used as a key intermediate in the production of various drugs, playing a crucial role in the development of new pharmaceuticals. Its chemical structure allows for the creation of a range of medicinal compounds with potential therapeutic applications.
Used in Agrochemical Production:
In the agrochemical industry, 2-Pyridinol,3-methoxy-(9CI) is utilized as an intermediate for the synthesis of pesticides and other agrochemicals. Its incorporation aids in the development of effective products designed to protect crops and enhance agricultural productivity.
Used in Organic Compound Synthesis:
Beyond its applications in pharmaceuticals and agrochemicals, 2-Pyridinol,3-methoxy-(9CI) is also employed in the synthesis of other organic compounds. Its versatility in chemical reactions makes it a valuable component in the creation of a diverse array of organic substances for various industrial applications.
Used in Medical Research:
2-Pyridinol,3-methoxy-(9CI) has been investigated for its potential use in the treatment of various medical conditions. Its pharmacological properties are of interest to researchers exploring new therapeutic avenues, particularly in the development of antifungal agents and other medicinal treatments.

InChI:InChI=1/C6H7NO2/c1-9-5-3-2-4-7-6(5)8/h2-4H,1H3,(H,7,8)

Upstream product

• 16867-04-2 dihydroxypyridine 
• 77-78-1 dimethyl sulfate 

Relevant academic research and scientific papers

Exploration of zinc-binding groups for the design of inhibitors for the oxytocinase subfamily of M1 aminopeptidases

The oxytocinase subfamily of M1 aminopeptidases consists of three members, ERAP1, ERAP2 and IRAP that play several important biological roles, including key functions in the generation of antigenic peptides that drive human immune responses. They represent emerging targets for pharmacological manipulation of the immune system, albeit lack of selective inhibitors is hampering these efforts. Most of the previously explored small-molecule binders target the active site of the enzymes via strong interactions with the catalytic zinc(II) atom and, while achieving increased potency, they suffer in selectivity. Continuing our earlier efforts on weaker zinc(II) binding groups (ZBG), like the 3,4-diaminobenzoic acid derivatives (DABA), we herein synthesized and biochemically evaluated analogues of nine potentially weak ZBGs, based on differential substitutions of functionalized pyridinone- and pyridinethione-scaffolds, nicotinic-, isonicotinic-, aminobenzoic- and hydrazinobenzoic-acids. Crystallographic analysis of two analogues in complex with a metalloprotease (MMP-12) revealed unexpected binding topologies, consistent with the observed affinities. Our results suggest that the potency of the compounds as inhibitors of ERAP1, ERAP2 and IRAP is primarily driven by the occupation of active-site specificity pockets and their proper orientation within the enzymes.