58076-33-8

Upstream product

• 2050-04-6 (pentyloxy)benzene 
• 110-53-2 1-Bromopentane 
• 108-95-2 phenol 
• 139-02-6 sodium phenoxide 
• 825-90-1 sodium p-hydroxybenzenesulfonate 

Downstream Products

• 1170071-73-4 N-(2-aminoethyl)-4-(pentyloxy)-benzenesulfonamide 
• 1160494-36-9 1-(ethynylsulfonyl)-4-(pentyloxy)benzene 
• 91216-77-2 4-pentyloxyphenylsulfonyl hydrazide 
• 101450-51-5 1-(4-pentyloxy-benzenesulfonyl)-piperidine 

Relevant academic research and scientific papers

METHODS OF USING SEMI-SYNTHETIC GLYCOPEPTIDES AS ANTIBACTERIAL AGENTS

Methods of using semi-synthetic glycopeptides of formula I-XIV having antibacterial activity are described.

NOVEL SEMI-SYNTHETIC GLYCOPEPTIDES AS ANTIBACTERIAL AGENTS

Semi-synthetic glycopeptides having antibacterial activity are described, in particular, the semi-synthetic glycopeptides described herein are made by chemical modification of the a glycopeptide (Compound A, Compound B, Compound H or Compound C) or the monosaccharide made by hydrolyzing the disaccharide moiety of the amino acid-4 of the parent glycopeptide in acidic medium to give the amino acid-4 monosaccharide; conversion of the monosaccharide to the amino-sugar derivative; acylation of the amino substituent on the amino acid-4 amino-substituted sugar moiety on these scaffolds with certain acyl groups; conversion of the amide group in amino acid-3 on these scaffolds to various acylamide, acylsulfonamide, acylsulfonylurea derivatives; aminomethylation with substituent containing sulfonamide or acylsulfonamide group on amino acid-7 through Mannich reaction; and conversion of the acid moiety on the macrocyclic ring of these scaffolds to certain substituted amides. Also provided are methods for the synthesis of the compounds, pharmaceutical compositions containing the compounds, and methods of use of the compounds for the treatment and/or prophylaxis of diseases, especially bacterial infections.

SEMI-SYNTHETIC GLYCOPEPTIDES HAVING ANTIBACTERIAL ACTIVITY

Semi-synthetic glycopeptides having antibacterial activity are described. Also described are processes of preparing such semi-synthetic glycopeptides by chemical modification of a glycopeptide (Compound A, Compound B, Compound H or Compound C) or the monosaccharide made by hydrolyzing the disaccharide moiety of the amino acid-4 of the parent glycopeptide in mild acidic medium to give the amino acid-4 monosaccharide; protection of the amino groups in the molecule; and conversion of the acid moiety on the macrocyclic ring of these scaffolds to certain substituted amides. Also included are the process of conversion of the amide group in amino acid-3 on these scaffolds to various acylureas, acylamide, acylsulfonamide, acylsulfonylurea derivatives and aminomethylation with substituent containing sulfonamide or acylsulfonamide group on amino acid-7 through Mannich reaction procedures. Further provided herein are pharmaceutical compositions containing the compounds, and methods of use of the compounds for the treatment and/or prophylaxis of diseases, including bacterial infections.

Synthesis of exo-3-ammo-7-azabicyclo[2.2.1]heptanes as a class of malarial aspartic protease inhibitors: Exploration of two binding pockets

The increasing prevalence of drug-resisLant strains of malaria-causing Plasmodium parasites necessitates the development of therapeutic agents that inhibit new biochemical targets. We herein describe the design, synthesis, and in vitro evaluation of a class of inhibitors that target the malarial aspartic proteases known as the plasmepsins. The title compounds feature a 7-azanorbornane skeleton that bears an exo-amino function, which was designed to interact with the catalytic dyad of aspartic proteases while providing vectors for the attachment of binding elements that target the flap and S1/S3 binding pockets at. the enzyme active site. Their synthesis takes advantage of a solvent-free and highly diastereoselective conjugate addition of amines to bicyclic vinyl sulfones. Structural optimization based on a little-known conformational preference of aryl sulfones produced the most potent inhibitors of this new class. In vitro assays demonstrate that the title compounds are capable of potent (IC50 ≥ 1.0 nM) inhibition of plasmepsins, while remaining relatively weak inhibitors of the closely related human enzymes cathepsins D and E. The ideal occupation of the flap pocket is crucial for both potency and selectivity over the human proteases. Differently functionalized compounds were synthesized to gain new insights info the molecular recognition properties of this cavity. Wiley-VCH Verlag GmbH & Co. KGaA.

Keratinocyte growth inhibitors and hydroxamic acid derivatives

This invention relates to a keratinocyte-proliferation inhibitor comprising as active ingredient a compound having an activity of inhibiting the solubilization of heparin-binding EGF-like growth factor bound to cell membranes and a compound of the formula (I); or pharmaceutically acceptable salt thereof, wherein R1, R2, R3 are hydrogen atom or alkyl and X is substituted benzene or the like.

The Effect of Two Terminal Alkoxy Groups on the Mesomorphic Properties of 4,4'-Disubstituted Phenylthiobenzoates

A select variety of homologs of the dialkoxyphenylthiobenzoates were prepared.Their mesomorphic properties were determined by hot-stage polarizing microscopy and compared with those for the analogous RO-R' and R-OR' thioesters and esters.Unlike