31898-69-8

Upstream product

• 108-05-4 vinyl acetate 
• 1189-71-5 isocyanate de chlorosulfonyle 
• 49639-35-2 3-(phenylsulfinyl)propionamide 
• 28562-53-0 4-acetoxy azetidinone 
• 108-98-5 thiophenol 
• 930-69-8 sodium thiophenolate 
• 344930-64-9 (2-oxo-4-phenylthioazetidin-1-yl)methyl benzoate 
• 934-87-2 S-phenyl thioacetate 
• 108-95-2 phenol 
• 97721-47-6 3-(phenylsulfanyl)propanamide 

Downstream Products

• 82342-06-1 2-(4-Oxo-azetidin-2-yl)-2-phenylsulfanyl-malonic acid dimethyl ester 
• 53390-58-2 4-(phenylsulfinyl)azetidin-2-one 
• 3111-52-2 potassium thiophenolate 
• 129314-70-1 Potassium; (E)-2-carbamoyl-ethenolate 
• 78902-62-2 (+/-)-1-(tert-butyldimethylsilyl)-4-phenylthio-2-azetidinone 
• 76060-84-9 N-<(methoxycarbonyl)methyl>-4-(phenylthio)azetidin-2-one 
• 188023-75-8 benzhydryl [2-13C]-2-[4'-(phenylthio)-2'-oxoazetidin-1'-yl]acetate 
• 701910-96-5 N-hydroxymethyl-4-phenylthioazetidin-2-one 
• 344930-64-9 (2-oxo-4-phenylthioazetidin-1-yl)methyl benzoate 
• 128624-96-4 4-(2-Chloro-1-hydroxymethyl-1-phenylsulfanyl-ethyl)-azetidin-2-one 
• 128624-95-3 4-(2-Hydroxy-1-hydroxymethyl-1-phenylsulfanyl-ethyl)-azetidin-2-one 
• 128624-97-5 5-Chloromethyl-2,2-dimethyl-5-phenylsulfanyl-3-oxa-1-aza-bicyclo[4.2.0]octan-8-one 
• 68960-65-6 1-methyl-4-phenylthioazetidin-2-one 

Relevant academic research and scientific papers

Non-transpeptidase binding arylthioether β-lactams active against Mycobacterium tuberculosis and Moraxella catarrhalis

The prevalence of drug resistance in both clinical and community settings as a consequence of alterations of biosynthetic pathways, enzymes or cell wall architecture is a persistent threat to human health. We have designed, synthesized, and tested a novel

SMALL MOLECULE ACTIVATORS AND INHIBITORS OF LECITHIN: CHOLESTEROL ACYLTRANSFERASE

The disclosure includes compounds and salts of Formula I, II, and III. The variables R, R0, R1, R10, R11, and R2 are defined herein. Compounds and salts of Formula I, II, and III are useful as modulat

C4-Alkylthiols with activity against Moraxella catarrhalis and Mycobacterium tuberculosis

Antimicrobial resistance represents a global threat to healthcare. The ability to adequately treat infectious diseases is increasingly under siege due to the emergence of drug-resistant microorganisms. New approaches to drug development are especially nee

Kinetics and Mechanism of Hydrolysis of N-Acyloxymethyl Derivatives of Azetidin-2-one

The pH-independent, acid-catalyzed and base-catalyzed hydrolyses of N-acyloxymethylazetidin-2-ones all occur at the ester function. The pH-independent hydrolysis involves rate-limiting alkyl C-O fission and formation of an exocyclic β-lactam iminum ion. This iminium ion is then trapped by water at the exocyclic iminium carbon atom, rather than at the β-lactam carbonyl carbon atom, to form the corresponding N-hydroxymethylazetidin-2-ones. Calculations carried out at the B3LYP/6-31+G(d) level of theory also support that nucleophilic attack by water takes place at the exocyclic carbon rather than at the β-lactam carbonyl carbon of the iminium ion. The mechanism for the acid-catalyzed pathway involves a preequilibrium protonation, probably at the β-lactam nitrogen, followed by rate-limiting alkyl C-O fission with formation of an exocyclic iminum ion. The base-catalyzed hydrolysis involves rate-limiting hydroxide attack at the ester carbonyl carbon. These results imply formation of a β-lactam system containing a positively charged amide nitrogen atom that hydrolyzes via a pathway that preserves the β-lactam structure in the product and provide further evidence that cleavage of the β-lactam C-N bond is not as facile as is commonly imagined.

The azomethine ylide strategy for β-lactam synthesis. An evaluation of alternative pathways for azomethine ylide generation

Following the generation of azomethine ylide 3 from the β-lactam-based oxazolidinone 1, a series of alternative entries to this and related 1,3-dipoles have been explored. The first approach is based on the use of monocyclic azetidinones 6-12 and 14 carrying a leaving group at C(4) and an activated (acidic) proton adjacent to the ring nitrogen, structural moieties which are both associated with 1. These monocyclic substrates show no tendency towards azomethine ylide formation, which points towards the ring strain present in 1 as an important prerequisite for azomethine ylide formation. The reactivity associated with the racemic Glaxo betaine 17, the structure of which has now been confirmed by X-ray crystallography, appears to involve an azomethine ylide 19, which is very similar to 3. However, attempts to trap 19 using an intermolecular cycloaddition failed; the intramolecular process involving an enolate as a trapping agent to give oxapenem 18 is more effective. Two novel thia-substituted bicyclic oxazolidinones 22 and 23, as well as the unsubstituted variant 33, have been prepared. In the case of 22 and 23, products derived from an alternative mode of iminium ion formation are observed. This pathway is a consequence of C-S bond cleavage, and this reactivity profile has been evaluated computationally. The data suggest that relief of strain within the four-membered ring-as opposed to 1 in which five-membered ring cleavage leads to an iminium ion-provides a driving force for C-S bond cleavage. As a result, the ability of 22 and 23 to give a synthetically useful azomethine ylide is compromised by the siting of an alternative leaving group adjacent to the azetidinone nitrogen. The unsubstituted bicyclic oxazolidinone 33 is thermally unstable, and no cycloadducts have been characterized from this system. Again, computational studies suggest that both direct and stepwise decarboxylation of 33 are energetically demanding processes.

Design, synthesis and stability of N-acyloxymethyl- and N-aminocarbonyloxymethyl-2-azetidinones as human leukocyte elastase inhibitors

A series of N-acyloxymethyl- and N-aminocarbonyloxymethyl derivatives of 2-azetidinones, 3, with different substituent patterns at the β-lactam C-3 and C-4 positions, were designed as potential mechanism-based inhibitors for human leukocyte elastase and f

Inhibition of serine proteases: Activity of 1,3-diazetidine-2,4-diones

The present work demonstrates that the 1,3-diazetidine-2,4-dione nucleus is effective as a scaffold of serine protease inhibitors. Compound 1 displayed high activity against human cathepsin G and α-chymotrypsin (0.39, 0.69 nM). Compound 6 exhibited 0.85 nM inhibition of human chymase. Compound 10 was a selective inhibitor against human neutrophil elastase.

Inhibition of human cytomegalovirus protease N(o) with monocyclic β- lactams

Monocyclic β-lactams have been identified as potent and selective inhibitors of the human cytomegalovirus protease (HCMV) N(o). Two series of these inhibitors are described, a peptidyl series of compounds and non- peptidic molecules featuring lower molecular weights. The SAR work that lead to the discovery of these inhibitors, together with their synthesis is also disclosed.

Possible biomimetic synthesis of β-lactams

The first successful syntheses of β-lactams via a Pummerer rearrangement of the corresponding sulfoxides are described. Thus, variously substituted 3-(phenylsulfinyl)propionamides were converted to 4-(phenylthio)-2-azetidinones in 14-50% yields with trime