105537-53-9

Upstream product

• 298-12-4 Glyoxilic acid 
• 103-79-7 1-phenyl-acetone 

Downstream Products

• 664336-40-7 5-phenylamino-5-methyl-4-phenyl-2(5H)-furanone 
• 664336-51-0 5-hydroxy-5-methyl-4-phenyl-1,5-dihydro-2H-pyrrol-2-one 
• 1160296-31-0 5-chloro-5-methyl-4-phenyl-2(5H)furanone 
• 105538-15-6 6-Amino-1-(3-ethoxycarbonyl-propyl)-3-methyl-4-phenyl-pyridazin-1-ium; bromide 
• 105537-67-5 6-Amino-1-(3-carboxy-propyl)-3-methyl-4-phenyl-pyridazin-1-ium; bromide 
• 105538-79-2 6-Chloro-3-methyl-4-phenyl-pyridazine 
• 140149-38-8 (6-Methyl-5-phenyl-pyridazin-3-yl)-hydrazine 
• 105537-98-2 3-amino-5-phenyl-6-methylpyridazine 
• 63795-91-5 5-phenyl-6-methyl-3(2H)-pyridazinone 

Relevant academic research and scientific papers

Thioether-linked dihydropyrrol-2-one analogues as PqsR antagonists against antibiotic resistant Pseudomonas aeruginosa

The Pseudomonas quinolone system (pqs) is one of the key quorum sensing systems in antibiotic-resistant P. aeruginosa and is responsible for the production of virulence factors and biofilm formation. Thus, synthetic small molecules that can target the PqsR (MvfR) receptor can be utilized as quorum sensing inhibitors to treat P. aeruginosa infections. In this study, we report the synthesis of novel thioether-linked dihydropyrrol-2-one (DHP) analogues as PqsR antagonists. Compound 7g containing a 2-mercaptopyridyl linkage effectively inhibited the pqs system with an IC50 of 32 μM in P. aeruginosa PAO1. Additionally, these inhibitors significantly reduced bacterial aggregation and biofilm formation without affecting planktonic growth. The molecular docking study suggest that these inhibitors bind with the ligand binding domain of the MvfR as a competitive antagonist.

Dihydropyrrolones as bacterial quorum sensing inhibitors

Bacteria regulate their pathogenicity and biofilm formation through quorum sensing (QS), which is an intercellular communication system mediated by the binding of signaling molecules to QS receptors such as LasR. In this study, a range of dihydropyrrolone (DHP) analogues were synthesized via the lactone-lactam conversion of lactone intermediates. The synthesized compounds were tested for their ability to inhibit QS, biofilm formation and bacterial growth of Pseudomonas aeruginosa. The compounds were also docked into a LasR crystal structure to rationalize the observed structure-activity relationships. The most active compound identified in this study was compound 9i, which showed 63.1% QS inhibition of at 31.25 μM and 60% biofilm reduction at 250 μM with only moderate toxicity towards bacterial cell growth.

NOVEL LACTAMS

The present invention relates to novel lactams of formulae (I) and (II). The present invention further relates to the use of these compounds in the treatment of microbial infections and microbial contamination of surfaces, particularly infections and surf

Synthesis and Structure-Activity Relationships of Series of Aminopyridazine Derivatives of γ-Aminobutyric Acid Acting as Selective GABA-A Antagonists

We have recently shown that an aryloaminopyridazine derivarive of GABA, SR 95103 , is a selective and competitive GABA-A receptor antagonist.In order to further explore the structural requirements for GABA receptor affinity, we synthesized a series of 38 compounds by attaching various pyridazinic structures to GABA or GABA-like side chains.Most of the compounds displaced GABA from rat brain membranes.All the active compounds antagonized the GABA-elicited enhancement of diazepam binding, strongly suggesting that all these compounds are GABA-A receptor antagonists.None of the compounds that displaced GABA from rat brain membranes interacted with other GABA recognition sites (GABA-B receptor, GABA uptake binding site, glutamate decarboxylase, GABA-transaminase).They did not interact with the Cl- ionophore associated with the GABA-A receptor and did not interact with the benzodiazepine, strychnine, and glutamate binding sites.Thus these compounds appear to be specific GABA-A receptor antagonists.In terms of structure-activity, it can be concluded that a GABA moiety bearing a positive charge is necessary for optimal GABA-A receptor recognition.Additional binding sites are tolerated only if they are part of a charge-delocalized amidinic or guanidinic system.If this delocalization is achieved by linking a butyric acid moiety to the N(2) nitrogen of a 3-aminopyridazine, GABA-antagonistic character is produced.The highest potency (ca.250 times bicuculline) was observed when an aromatic ? system, bearing electron-donating substituents, was present on the 6-position of the pyridazine ring.