85849-94-1

Usage

InChI:InChI=1/C11H15NO4S/c1-8(2)10(11(13)14)12-17(15,16)9-6-4-3-5-7-9/h3-8,10,12H,1-2H3,(H,13,14)/p-1/t10-/m1/s1

Upstream product

• 72-18-4 L-valine 
• 191792-79-7 (S)-2-benzenesulfonylamino-3-methylbutyric acid ethyl ester 
• 17431-03-7 L-valine ethyl ester 
• 98-09-9 benzenesulfonyl chloride 

Downstream Products

• 270071-99-3 (S)-2-(Benzenesulfonyl-benzyl-amino)-3-methyl-butyric acid 
• 197521-39-4 (S)-2-Benzenesulfonylamino-3-methyl-butyric acid methyl ester 
• 543725-75-3 N-{(S)-1-[1-(4-Chloro-phenyl)-meth-(E)-ylidene-hydrazinocarbonyl]-2-methyl-propyl}-benzenesulfonamide 
• 543725-68-4 N-[2-methyl-1-(3-methyl-5-oxo-4,5-dihydro-pyrazole-1-carbonyl)-propyl]-benzenesulfonamide 
• 543725-60-6 N-(1-hydrazinocarbonyl-2-methyl-propyl)-benzenesulfonamide 

Relevant academic research and scientific papers

Synthesis and biological evaluation of Val–Val dipeptide–sulfonamide conjugates

Novel Val–Val dipeptide–benzenesulfonamide conjugates were reported in this study. These were achieved by a condensation reaction of p-substituted benzenesulfonamoyl alkanamides with 2-amino-4-methyl-N-substituted phenyl butanamide using classical peptide

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 of novel heterocyclic sulfonamides as protease inhibitors of HIV-1

Background: HIV-1 protease is a prime target for drug therapy due to its integral role in HIV viral replication. Several protease inhibitors such as lopinavir and tipranavir were shown to possess potent inhibitory activities against the HIV virus. Due to the high mutation rate of HIV, resistance remains a major problem in the treatment of this virus and design and synthesis of new protease inhibitors is an area of continued interest in new drug discovery research. Methods: Utilizing the key fragments of structures of both peptide-based and non-peptide-based protease inhibitors lopinavir and tipranavir, we explored designing some new compounds. Results: Six new protease inhibitors were designed and synthesized based on the key structural fragments in lopinavir and tipranavir. The designed new compounds contain heterocyclic groups such as thiophene, isoxazole, and imidazole groups, and the best compound exhibited 0.6 nm of the protease inhibitory activity. Conclusion: We have prepared some novel heterocyclic sulfonamides utilizing a key fragment based approach by recombining structural fragments of the potent protease inhibitors lopinavir and tipranavir. Some of these newly designed compounds showed good to excellent HIV-1 protease inhibitory activity, which indicated that this method would be useful for the discovery of new drug lead compounds that target HIV.

Controlling Plasma Stability of Hydroxamic Acids: A MedChem Toolbox

Hydroxamic acids are outstanding zinc chelating groups that can be used to design potent and selective metalloenzyme inhibitors in various therapeutic areas. Some hydroxamic acids display a high plasma clearance resulting in poor in vivo activity, though they may be very potent compounds in vitro. We designed a 57-member library of hydroxamic acids to explore the structure-plasma stability relationships in these series and to identify which enzyme(s) and which pharmacophores are critical for plasma stability. Arylesterases and carboxylesterases were identified as the main metabolic enzymes for hydroxamic acids. Finally, we suggest structural features to be introduced or removed to improve stability. This work thus provides the first medicinal chemistry toolbox (experimental procedures and structural guidance) to assess and control the plasma stability of hydroxamic acids and realize their full potential as in vivo pharmacological probes and therapeutic agents. This study is particularly relevant to preclinical development as it allows obtaining compounds equally stable in human and rodent models.

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.

Evaluation of Antibacterial and Antifungal Effects of Novel Hydroxamic Acids Linked-natural Amino Acids

A SERIES of new derivatives containing hydroxamic acids linked-amino acids has been synthesized and fully characterized by spectroscopic techniques including; 1H, 13C, DEPT 135 and HRMS.These new compounds were tested for their antib

Synthesis, characterization and antifungal activities of some benzenesulphonylamino acid derivatives

Condensation of benzenesulphonyl chloride (1) with a series of amino acids afforded benzenesulphonylamino acids (2a-d). Esterification of the derivatives (2a-d) in methanol gave the corresponding benzensulphonylamino acid methylesters (3a-d), which conden

Structure-based design and synthesis of potent matrix metalloproteinase inhibitors derived from a 6H-1,3,4-thiadiazine scaffold

We describe a new generation of heterocyclic nonpeptide matrix metalloproteinase (MMP) inhibitors derived from a 6H-1,3,4-thiadiazine scaffold. A screening effort was utilized to identify some chiral 6-methyl-1,3,4-thiadiazines that are weak inhibitors of

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.