270073-00-2

Upstream product

• 72-18-4 L-valine 
• 98-74-8 4-Nitrobenzenesulfonyl chloride 

Downstream Products

• 270072-06-5 (S)-2-[Benzyl-(4-nitro-benzenesulfonyl)-amino]-3-methyl-butyric acid 
• 852853-21-5 N^α-nosyl-L-valine chloride 
• 103478-58-6 Fmoc-N-methylvaline 
• 852853-12-4 N-(N-(N-nosyl-L-valyl)-N-methyl-L-isoleucyl)-L-alanine methyl ester 
• 852853-11-3 N-(N-(N-nosyl-L-valyl)-N-methyl-D-phenylalanyl)-L-alanine methyl ester 
• 852853-10-2 N-(N-(N-nosyl-L-valyl)-N-methyl-L-phenylalanyl)-L-alanine methyl ester 
• 1208119-44-1 N-nosyl-L-valine phenacyl ester 
• 1220527-23-0 N-nosyl-L-valine benzhydryl ester 

Relevant academic research and scientific papers

Synthesis, characterization and in vitro antitrypanosomal activities of new carboxamides bearing quinoline moiety

The reported toxicities of current antitrypanosomal drugs and the emergence of drug resistant trypanosomes underscore the need for the development of new antitrypanosomal agents. We report herein the synthesis and antitrypanosomal activity of 24 new amide derivatives of 3-aminoquinoline, bearing substituted benzenesulphonamide. Nine of the new derivatives showed comparable antitrypanosomal activities at IC50 range of 1–6 nM (melarsoprol 5 nM). Compound 11n and 11v are more promising antitrypanosomal agents with IC50 1.0 nM than the rest of the reported derivatives. The novel compounds showed satisfactory predicted physico-chemical properties including oral bioavailability, permeability and transport properties.

Synthesis and anticancer activity of the proposed structure of caldoramide, an N-peptidyltetramate from the cyanobacterium Caldora penicillata

The structure proposed in the literature for caldoramide, a formal pentapeptide metabolite of the marine cyanobacterium Caldora penicillata, was synthesised in 12 steps and 16% yield (longest linear sequence from isoleucine) following the strategy of a stepwise consecutive extension of an N-oligopeptidyl chain on a tetramate anchor. The synthetic product differed from the natural isolate in optical rotation, some NMR data, and cytotoxicities. Its antiproliferative effect on three human cancer cell lines was distinctly lower than that of related dolastatin 10 and belamide A.

Novel anti-inflammatory and analgesic agents: synthesis, molecular docking and in vivo studies

Twelve new derivatives of benzothiazole bearing benzenesulphonamide and carboxamide were synthesised and investigated for their in vivo anti-inflammatory, analgesic and ulcerogenic activities. Molecular docking showed an excellent binding interaction of t

Synthesis, characterization, molecular docking and in?vitro antimalarial properties of new carboxamides bearing sulphonamide

Sulphonamides and carboxamides have shown large number of pharmacological properties against different types of diseases among which is malaria. Twenty four new carboxamide derivatives bearing benzenesulphonamoyl alkanamides were synthesized and investigated for their in silico and in?vitro antimalarial and antioxidant properties. The substituted benzenesulphonyl chlorides (1a-c) were treated with various amino acids (2a-h) to obtain the benzenesulphonamoyl alkanamides (3a-x) which were subsequently treated with benzoyl chloride to obtain the N-benzoylated derivatives (5a-f, i-n and q-v). Further reactions of the N-benzoylated derivatives or proline derivatives with 4-aminoacetophenone (6) using boric acid as a catalyst gave the sulphonamide carboxamide derivatives (7a-x) in excellent yields. The in?vitro antimalarial studies showed that all synthesized compounds had antimalarial property. Compound 7k, 7c, 7l, 7s, and 7j had mean MIC value of 0.02, 0.03, 0.05, 0.06 and 0.08?μM respectively comparable with chloroquine 0.06?μM. Compound 7c was the most potent antioxidant agent with IC50 value of 0.045?mM comparable with 0.34?mM for ascorbic acid. In addition to the successful synthesis of the target molecules using boric acid catalysis, the compounds were found to have antimalarial and antioxidant activities comparable with known antimalarial and antioxidant drugs. The class of compounds reported herein have the potential of reducing oxidative stress arising from malaria parasite and chemotherapeutic agent used in the treatment of malaria.

New carboxamide derivatives bearing benzenesulphonamide as a selective COX-II inhibitor: Design, synthesis and structure-activity relationship

Sixteen new carboxamide derivatives bearing substituted benzenesulphonamide moiety (7a-p) were synthesized by boric acid mediated amidation of appropriate benzenesulphonamide with 2-amino-4-picoline and tested for anti-inflammatory activity. One compound 7c showed more potent anti-inflammatory activity than celecoxib at 3 h in carrageenan-induced rat paw edema bioassay. Compounds 7g and 7k also showed good anti-inflammatory activity comparable to celecoxib. Compound 7c appeared selectivity index (COX-2/COX-1) better than celecoxib. Compound 7k appeared selectivity index (COX-2/COX-1) a little higher than the half of celecoxib while compound 7g is non-selective for COX-2. The LD50 of compounds 7c, 7g and 7k were comparable to celecoxib.

The dimethylsulfoxonium methylide as unique reagent for the simultaneous deprotection of amino and carboxyl function of N-Fmoc-α-amino acid and N-Fmoc-peptide esters

The dimethylsulfoxonium methylide is described as a unique and useful reagent for the simultaneous deprotection of amino and carboxyl function of N-Fmoc-α-amino acid and N-Fmoc-peptide esters. The new methodology was applied successfully both to solution- and solid-phase peptide synthesis. The adopted methodology was extended successfully also to peptides containing amino acids bearing acid-sensitive protecting group in side chains. Furthermore no measurable epimerization was observed in the deprotection reaction of N-Fmoc-dipeptide methyl esters with dimethylsulfoxonium methylide.

N-methyl-N-nosyl-β3-amino acids

(Chemical Equation Presented) N-Methyl-β3-amino acids are important building blocks in the synthesis of biologically active molecules. A very simple and efficient approach to transform natural α-amino acids into their corresponding N-methyl-βs

N-methylation of peptides on selected positions during the elongation of the peptide chain in solution phase

An efficient and general solution-phase method for the site-specific N-methylation of peptides has been developed. This novel procedure involves synthesis of N-nosyl protected peptides and their subsequent N-methylation with diazomethane. Its efficiency w

Protease inhibitors. Part 7: Inhibition of Clostridium histolyticum collagenase with sulfonylated derivatives of L-valine hydroxamate

Sulfonylated L-valine hydroxamate derivatives were obtained by reaction of alkyl/arylsulfonyl halides with the title amino acid, followed by treatment with benzyl chloride, and conversion of the COOH moiety to the CONHOH group. Other derivatives were obtained by reaction of N-benzyl-L- valine with arylisocyanates, arylsulfonylisocyanates or benzoylisothiocyanate, followed by the similar conversion of the COOH into the CONHOH moiety, with hydroxylamine in the presence of carbodiimides. The obtained compounds were assayed as inhibitors of the Clostridium histolyticum collagenase, ChC (EC 3.4.24.3), a zinc enzyme which degrades triple helical collagen. The hydroxamate derivatives were generally 100-500 times more active than the corresponding carboxylates. In the series of synthesized derivatives, substitution patterns leading to best ChC inhibitors were those involving perfluoroalkylsulfonyl- and substituted-arylsulfonyl moieties, such as pentafluorophenylsulfonyl; 3- and 4-protected-aminophenylsulfonyl-; 3- and 4-carboxyphenylsulfonyl-; 3-trifluoromethylphenylsulfonyl; or 1- and 2- naphthyl among others. Similarly to the matrix metalloproteinase hydroxamate inhibitors, ChC inhibitors of the type reported here must incorporate hydrophobic moieties at the P(2') and P(3') subsites, in order to achieve tight binding to the enzyme. Such compounds might lead to drugs useful in the treatment corneal bacterial keratitis. (C) 2000 Elsevier Science B.V.