100949-02-8

Basic information

• Product Name: Nicotinonitrile, 5-vinyl- (6CI)
• Synonyms: Nicotinonitrile, 5-vinyl- (6CI)
• CAS NO: 100949-02-8
• Molecular Formula: C₈H₆N₂
• Molecular Weight: 130.14664
• Product Categories: PYRIDINE
• Mol File: 100949-02-8.mol
• Article Data: 6

Chemical Properties

• Appearance: /
• CAS DataBase Reference: Nicotinonitrile, 5-vinyl- (6CI)(CAS DataBase Reference)
• NIST Chemistry Reference: Nicotinonitrile, 5-vinyl- (6CI)(100949-02-8)
• EPA Substance Registry System: Nicotinonitrile, 5-vinyl- (6CI)(100949-02-8)

Safety Data

• Hazardous Substances Data: 100949-02-8(Hazardous Substances Data)

Upstream product

• 35590-37-5 5-bromopyridine-3-carbonitrile 
• 7486-35-3 tri-n-butyl(vinyl)tin 

Downstream Products

• 562074-59-3 5-(chloromethyl)nicotinonitrile hydrochloride 
• 135124-71-9 5-(hydroxymethyl)pyridine-3-carbonitrile 
• 70416-53-4 5-formylpyridine-3-carbonitrile 

Relevant articles and documents

Mur ligases inhibitors with azastilbene scaffold: Expanding the structure–activity relationship

Antibiotic resistance represents one of the biggest public health challenges in the last few years. Mur ligases (MurC–MurF) are involved in the synthesis of UDP-N-acetylmuramyl-pentapeptide, the main building block of bacterial peptidoglycan polymer. They are essential for the survival of bacteria and therefore important antibacterial targets. We report herein the synthesis and structure–activity relationships of Mur ligases inhibitors with an azastilbene scaffold. Several compounds showed promising inhibitory potencies against multiple ligases and one compound also possessed moderate antibacterial activity. These results represent a solid ground for further development and optimization of structurally novel antimicrobial agents to combat the rising bacterial resistance.

Evaluation of the published kinase inhibitor set to identify multiple inhibitors of bacterial ATP-dependent mur ligases

The Mur ligases form a series of consecutive enzymes that participate in the intracellular steps of bacterial peptidoglycan biosynthesis. They therefore represent interesting targets for antibacterial drug discovery. MurC, D, E and F are all ATP-dependent ligases. Accordingly, with the aim being to find multiple inhibitors of these enzymes, we screened a collection of ATP-competitive kinase inhibitors, on Escherichia coli MurC, D and F, and identified five promising scaffolds that inhibited at least two of these ligases. Compounds 1, 2, 4 and 5 are multiple inhibitors of the whole MurC to MurF cascade that act in the micromolar range (IC50, 32–368 μM). NMR-assisted binding studies and steady-state kinetics studies performed on aza-stilbene derivative 1 showed, surprisingly, that it acts as a competitive inhibitor of MurD activity towards D-glutamic acid, and additionally, that its binding to the D-glutamic acid binding site is independent of the enzyme closure promoted by ATP.

BICYCLIC COMPOUNDS AS INHIBITORS OF PD1/PD-L1 INTERACTION/ACTIVATION

The compounds of Formula I is described herein along with their polymorphs, stereoisomers, tautomers, prodrugs, solvates, and pharmaceutically acceptable salts thereof. The compounds described herein, their polymorphs, stereoisomers, tautomers, prodrugs, solvates, and pharmaceutically acceptable salts thereof are bicyclic compounds that are inhibitors of PD-1/PD-L1 interaction/activation.