80395-50-2

Upstream product

• 6285-57-0 2-amino-6-nitrobenzothiazole 
• 108-24-7 acetic anhydride 
• 75-36-5 acetyl chloride 
• 100-01-6 4-nitro-aniline 
• 66934-12-1 N-(4-nitrophenyl)-N'-acetylthiourea 
• 3696-22-8 p-nitrophenylthiourea 
• 136-95-8 2-amino-benzthiazole 

Downstream Products

• 546076-59-9 6-nitro-[3-(furan-2-yl)-prop-2-eneamido]benzothiazole 
• 1213251-06-9 6-nitro-[3-(3-hydroxy-4-methoxyphenyl)-prop-2-eneamido]-benzothiazole 
• 466649-86-5 6-nitro-[3-(4-chlorophenyl)-prop-2-eneamido]benzothiazole 
• 349433-28-9 6-nitro-[3-phenyl-prop-2-eneamido]benzothiazole 
• 1213251-05-8 6-nitro-[3-(4-hydroxyphenyl)-prop-2-eneamido]benzothiazole 
• 466649-82-1 6-nitro-[3-(4-methoxyphenyl)-prop-2-eneamido]benzothiazole 

Relevant academic research and scientific papers

Exploring the Chemical Space of Benzothiazole-Based DNA Gyrase B Inhibitors

We designed and synthesized a series of inhibitors of the bacterial enzymes DNA gyrase and DNA topoisomerase IV, based on our recently published benzothiazole-based inhibitor bearing an oxalyl moiety. To improve the antibacterial activity and retain potent enzymatic activity, we systematically explored the chemical space. Several strategies of modification were followed: varying substituents on the pyrrole carboxamide moiety, alteration of the central scaffold, including variation of substitution position and, most importantly, modification of the oxalyl moiety. Compounds with acidic, basic, and neutral properties were synthesized. To understand the mechanism of action and binding mode, we have obtained a crystal structure of compound 16a, bearing a primary amino group, in complex with the N-terminal domain of E. coli gyrase B (24 kDa) (PDB: 6YD9). Compound 15a, with a low molecular weight of 383 Da, potent inhibitory activity on E. coli gyrase (IC50 = 9.5 nM), potent antibacterial activity on E. faecalis (MIC = 3.13 μM), and efflux impaired E. coli strain (MIC = 0.78 μM), is an important contribution for the development of novel gyrase and topoisomerase IV inhibitors in Gram-negative bacteria.

NOVEL HYDRAZONE DERIVATIVE WITH ARYL OR HETEROARYL GROUP SUBSTITUTED AT TERMINAL AMINE GROUP THEREOF AND USE THEREOF

The present invention relates to novel hydrazone derivatives in which a terminal amine group is substituted with an aryl group or a heteroaryl group, and uses thereof.

From Bacteria to Cancer: A Benzothiazole-Based DNA Gyrase B Inhibitor Redesigned for Hsp90 C-Terminal Inhibition

Heat shock protein 90 (Hsp90) is a molecular chaperone that is responsible for the folding and maturation of client proteins that are associated with all ten hallmarks of cancer. Hsp90 N-terminal pan inhibitors have experienced unfavorable results in clinical trials due to induction of the heat shock response (HSR), among other concerns. Novobiocin, a well characterized DNA gyrase B inhibitor, was identified as the first Hsp90 C-terminal inhibitor that manifested anticancer effects without induction of the HSR. In this letter, a library of Hsp90 C-terminal inhibitors derived from a benzothiazole-based scaffold, known to inhibit DNA gyrase B, was designed, synthesized, and evaluated. Several compounds were found to manifest low micromolar activity against both MCF-7 and SKBr3 breast cancer cell lines via Hsp90 C-terminal inhibition.

Novel hydrazone derivatives comprising aryl or heteroaryl group substituted at terminal amine and use thereof

The present invention relates to novel hydrazone derivatives with an aryl or heteroaryl group substituted at a terminal amine group thereof and a use thereof.

Synthesis, ADMET Properties, and Biological Evaluation of Benzothiazole Compounds Targeting Chemokine Receptor 2 (CXCR2)

Herein we describe the synthesis and biological evaluation of a series of novel benzothiazoles based on a diaryl urea scaffold previously reported in some allosteric chemokine receptor 2 (CXCR2) inhibitors. From a library of 41 new compounds, 17 showed significant inhibition of CXCR2, with IC50 values less than 10 μm and selectivity over CXCR4. Our ADMET simulations suggest favorable drug-like properties for the active compounds. Importantly, we developed a predictive model that can distinguish active from inactive compounds; this will serve as a valuable tool to guide the design of optimized compounds to be evaluated in preclinical models.

Probing the ATP-Binding Pocket of Protein Kinase DYRK1A with Benzothiazole Fragment Molecules

DYRK1A has emerged as a potential target for therapies of Alzheimer's disease using small molecules. On the basis of the observation of selective DYRK1A inhibition by firefly d-luciferin, we have explored static and dynamic structural properties of fragment sized variants of the benzothiazole scaffold with respect to DYRK1A using X-ray crystallography and NMR techniques. The compounds have excellent ligand efficiencies and show a remarkable diversity of binding modes in dynamic equilibrium. Binding geometries are determined in part by interactions often considered "weak", including "orthogonal multipolar" types represented by, for example, F-CO, sulfur-aromatic, and halogen-aromatic interactions, together with hydrogen bonds that are modulated by variation of electron withdrawing groups. These studies show how the benzothiazole scaffold is highly promising for the development of therapeutic DYRK1A inhibitors. In addition, the subtleties of the binding interactions, including dynamics, show how full structural studies are required to fully interpret the essential physical determinants of binding.

Synthesis of N-benzothiazol-2-yl-amides by Pd-catalyzed C(sp2)-H functionalization

A catalytic synthesis of N-benzothiazol-2-yl-amides from 1-acyl-3-(phenyl)thioureas was achieved in the presence of a palladium catalyst through the C(sp2)-H functionalization/C-S bond formation. This synthetic methodology can produce various N

Synthesis and anti-cancer studies of 2, 6-disubstituted benzothiazole derivatives

On the basis of exhaustive literature review, it has been found that benzothiazole derivatives have good potential to exhibit anticancer activity15-17. So the present study involves the synthesis of 2,6-disubstituted benzothiazole followed by preliminary cytotoxicity screening against three human cancer cell lines(MCF-7, HeLa and MG63) using MTT assay at 48 h of exposure.

Synthesis of N-benzothiazol-2-yl-amides by an iron-catalyzed oxidative C(sp2)-H functionalization

Catalytic synthesis of N-benzothiazol-2-yl-amides from 1-acyl-3-(phenyl) thioureas was achieved in the presence of an iron catalyst through C(sp 2)-H functionalization and C-S bond formation. Various N-benzothiazol-2-yl-amides were selectively obtained in good yields. Georg Thieme Verlag Stuttgart, New York.

Mechanism of oxidation of N-aryl-N'-acylthioureas

The synthesis of N-2-(6-methoxy/6-nitrobenzothiazolyl)-N,N'-diacyl-N''-(4- methoxy/4-nitrophenyl)-guanidine (4) and 2-acetylamino-6-acetylamino-6-(methoxy/ nitro)-benzothiazoles (5) from N-aryl-N'-acetylthioureas by oxidation under various conditions is described. The structure of products was confirmed by IR and NMR spectral evidence.