27727-70-4

Upstream product

• 100-39-0 benzyl bromide 
• 65-49-6 4-Aminosalicylic acid 
• 13684-28-1 2-hydroxy-4-nitro-benzoic acid methyl ester 
• 619-19-2 2-hydroxy-4-nitrobenzoic acid 
• 4136-97-4 methyl 4-aminosalicylate 

Downstream Products

• 1379520-47-4 C₂₉H₂₄N₂O₇ 
• 107351-59-7 2-benzyloxy-4-acetamidobenzoic acid methyl ester 
• 27475-15-6 4-(2-Bromo-acetyl)-2-hydroxy-benzoic acid methyl ester 
• 27475-11-2 methyl 4-acetyl-2-hydroxybenzoate 
• 24085-11-8 α¹-(Benzylisopropylamino)-methyl-3-hydroxy-p-xylol-α¹,α⁴-diol 
• 18910-67-3 3-Hydroxy-α¹-(isopropylamino)-methyl)-p-xylol-α¹,α⁴-diol 
• 27475-10-1 4-Acetyl-2-benzyloxy-benzoic acid methyl ester 
• 1393652-97-5 C₄₂H₃₇N₃O₇ 
• 1393652-95-3 C₄₃H₃₉N₃O₇ 
• 1393652-93-1 C₄₃H₃₇N₃O₉ 
• 1393652-91-9 C₃₃H₂₈N₂O₅ 
• 1393652-89-5 C₃₃H₂₆N₂O₇ 

Relevant academic research and scientific papers

Peptidomimetic analogues of an Arg-Trp-x-x-Trp motif responsible for interaction of translocase MraY with bacteriophage ?X174 lysis protein E

Translocase MraY is the target for bacteriophage ?X174 lysis protein E, which interacts via a protein–protein interaction mediated by Phe-288 and Glu-287 of E. coli MraY, and an Arg-Trp-x-x-Trp motif on protein E, also found in several cationic antimicrob

A New Series of Salicylic Acid Derivatives as Non-saccharide α-Glucosidase Inhibitors and Antioxidants

In this study, a series of salicylic acid derivatives were designed and synthesized as novel non-saccharide α-glucosidase inhibitors. Biological evaluation indicated that when compared to acarbose, compounds T9, T10, and T32 exhibited a higher potency of α-glucosidase inhibitory activity with IC50 values of 0.15±0.01, 0.086±0.01 and 0.32±0.02mM, respectively. Evaluation of the inhibition kinetics indicated that T9, T10, T32, and acarbose interacted with α-glucosidase in a mixed non-competitive inhibitory manner. Moreover, T9, T10, and T32 statically quenched the fluorescence of α-glucosidase by formation of an inhibitor-α-glucosidase complex. The docking results showed that hydrogen bonds were generated between the test compounds and α-glucosidase. The antioxidant study revealed that compound T10 exhibited a higher antioxidant activity via scavenging 1,1-diphenyl-2-picrylhydrazyl free radical (DPPH), thereby inhibiting lipid peroxidation and the total reduction capacity. In brief, the salicylic acid derivatives identified in this study were promising candidates for development as novel non-saccharide α-glucosidase inhibitors.

2-ARYLSULFONAMIDO-N-ARYLACETAMIDE DERIVATIZED STAT3 INHIBITORS

The present disclosure provides pharmaceutical compositions comprising 2-arylsulfonamido-N-arylacetamide derivatized Stat3 inhibitors and certain pharmaceutically acceptable salts thereof, and methods of their use.

SMALL MOLECULE INHIBITORS OF THE MCL-1 ONCOPROTEIN AND USES THEREOF

Compounds that inhibit Myeloid Cell Leukemia-1 (Mcl-1) oncoprotein, and methods of using the same, are provided for treating disease.

Conformational properties of O-alkylated benzamides

In this article, we report the synthesis, solid-state and solution-state conformational studies of O-alkylated aromatic benzamides based on two scaffolds. Intramolecular hydrogen bonding provides conformational pre-organization and side chains can interact with each other within a molecule. In the solid-state three-dimensional arrangement, the molecules further interact with each other through non-covalent interactions. Given, the demonstrated potential of this class of scaffolds to act as helix mimetics for the inhibition of protein-protein interactions (PPIs), these results provide key insight for future inhibitor design.