30929-24-9

Upstream product

• 104-88-1 4-chlorobenzaldehyde 
• 829-20-9 2',4'-dimethoxyacetophenone 

Downstream Products

• 125966-82-7 <4-(2,4-dimethoxyphenyl)-6-(4-chlorophenyl)>pyrimidine-2-sulphonamido-N⁴-acetamide 
• 1119306-87-4 C₂₃H₂₂ClN₃O₄S 
• 259086-68-5 4-(4-chlorophenyl)-6-(2,4-dimethoxyphenyl)pyrimidin-2-amine 
• 301325-28-0 C₂₃H₂₁ClN₂O₂ 

Relevant academic research and scientific papers

QSAR, in silico docking and in vitro evaluation of chalcone derivatives as potential inhibitors for H1N1 virus neuraminidase

Thirty three chalcones were synthesized and tested on viral H1N1 neuraminidase activity by using MUNANA assay [2′-(4-methylumbelliferyl)-α-d-N-acetylneuraminic acid] assay with DANA (2,3-didehydro-2-deoxy-N-acetylneuraminic acid) was used as standard. 2D and 3D-quantitative structure?activity relationship models have been successfully developed with a good correlative and predictive ability for quantitative structure?activity relationships of these chalcone derivatives. Result from the 2D-quantitative structure?activity relationship model indicates that electrostatic parameter enhanced bioactivity of the chalcones while steric substituents diminished their potency as H1N1 neuraminidase inhibitors. 3D-quantitative structure?activity relationship model showed the importance of the position of the hydroxyl group in chalcone derivatives which can influence on hydrophobicity, hydrogen bond donor and aromatic ring features that enhance the biological activity. Finally, docking studies showed that chalcones MC8 and MC16 with low C docker interaction energies and higher numbers of hydrogen bonding have better inhibitory activity against viral H1N1 neuraminidase.

Design, synthesis and evaluation of 2,4,6-substituted pyrimidine derivatives as BACE-1 inhibitor: Plausible lead for alzheimer’s disease

Alzheimer’s disease is one of the most common neurodegenerative disorder afflicting a large mass of population. BACE-1 (β-secretase) is an aspartyl protease of the amyloidogenic pathway considered responsible for Alzheimer’s disease (AD). Since it catalyzes the rate-limiting step of Aβ-42 production from amyloid precursor protein (APP), its inhibition is considered a viable thera-peutic strategy. We have reported the design of small molecular weight compounds supposed to be blood brain permeable as BACE-1 inhibitors. The clue for the design of this series is drawn from the previously designed series from our research group. Objective: Design and synthesis of 2,4,6-substituted pyrimidine derivatives has been reported. In vitro FRET-based screening of synthesized derivatives was performed to evaluate the BACE-1 inhibition profile. Methods: Based on the docking simulation studies, a library of derivatives was designed, synthesized and evaluated for BACE-1 inhibition in-vitro. The docking studies were performed on Glide (Schrodinger suite) and Molegro virtual docker. Theoretical toxicity was predicted using Osiris Property Explorer. The synthesized compounds were tested for BACE-1 inhibition using in vitro assay based on Fluorescence Resonance Energy Transfer technique. The percent inhibition was cal-culated as a measure of activity. Results: The designed compounds revealed strong interactions with the desired amino acids of BACE-1 active sites. The aromatic rings placed at the fourth and sixth position of the pyrimidine ring occupied S1 and S3 substrate-binding clefts while the amino group formed hydrogen bonding interactions with Asp32 and Asp228. In silico data ensured that the compounds were orally bioavailable and brain permeable. The in vitro testing showed that the compounds inhibited BACE-1 at 10μM concentration. Conclusion: Compounds substituted with m-benzyloxy on one aromatic ring and o,p-di-chloro on another aromatic ring displayed maximum BACE-1 inhibition. Compound 2.13A displayed high docking score and was found to be most potent with IC50 of 6.92μM. The series displayed a good correlation between the docking score and BACE-1 inhibition profile.

Discovery of N-pyridoyl-Δ2-pyrazolines as Hsp90 inhibitors

Hsp90, as a key molecular chaperone, plays an important role in modulating the activity of many cell signaling proteins and is an attractive target for anticancer therapeutics. Herein, we report the discovery of N-pyridoyl-Δ2-pyrazoline analogs

Synthesis, molecular docking and α-glucosidase inhibitory activity study of 2,4,6-triaryl pyrimidine derivatives

Background: α-Glucosidase inhibitors hinder the carbohydrate digestion and play an important role in the treatment of diabetes mellitus. α-glucosidase inhibitors available on the market are acarbose, miglitol, and voglibose. However, the use of acarbose is diminishing due to related side effects like diarrhea, bloating and abdominal distension. Objectives: This study aimed to synthesize 2,4,6-triaryl pyrimidines derivatives, screen their α-glucosidase inhibitory activity, perform kinetic and molecular docking studies. Methods: A series of 2,4,6-triaryl pyrimidine derivatives were synthesized and their α-glucosidase inhibitory activity was screened in vitro. Pyrimidine derivatives 4a-m were synthesized via a two-step reaction with a yield between 49 and 93%. The structure of the synthesized compounds was confirmed by different spectroscopic techniques (IR, NMR and MS). The in vitro α-glucosidase inhibition activities of the synthesized compounds 4a-m was also evaluated against Saccharomyces cerevisiae α-glucosidase. Results and Discussion: The majority of synthesized compounds had α-glucosidase inhibitory activity. Particularly compounds 4b and 4g were the most active compounds with an IC50 value of 125.2± 7.2 and 139.8 ± 8.1 μM respectively. The kinetic study performed for the most active compound 4b revealed that the compound was a competitive inhibitor of Saccharomyces cerevisiae α-glucosidase with Ki of 122 μM. The molecular docking study also revealed that the two compounds have important binding interactions with the enzyme active site. Conclusion: 2,4,6-triarylpyrimidine derivative 4a-m were synthesized and screened for α-glucosidase inhibitory activity. Most of the synthesized compounds possess α-glucosidase inhibitory activity, and compound 4b demonstrated the most significant inhibitory action as compared to acarbose.

Novel chalcones and 1,3,5-triphenyl-2-pyrazoline derivatives as antibacterial agents

Novel sixteen chalcones and thirteen 1,3,5-triphenyl-2-pyrazolines were synthesized and characterized using FT-IR, HR-Mass, NMR (1H-NMR, 13C-NMR, 135 DEPT, 1H-1H CoSY and 1H and 13C CoSY) a

Synthesis and antiinflammatory activity of some new 1,3,5-trisubstituted pyrazolines bearing benzene sulfonamide

Nineteen new 2-pyrazoline bearing benzenesulfonamide derivatives were synthesized by condensing chalcones with 4-hydrazinonbenzenesulfonamide hydrochloride. Their chemical structures were proved by means of IR, 1H NMR, 13C NMR, mass spectroscopic and elemental analyses data. These compounds were tested at dose of 20 mg/kg for their anti-inflammatory activity in carrageenan-induced rat paw edema model and volume of paw edema was measured at 0, 3 and 5 h. Two compounds 3k and 3l were found to be more active than celecoxib throughout the study (at 3 and 5 h). While two other compounds 3m and 3n showed more potent activity than celecoxib at 5 h. They are devoid of ulcerogenic potential when administered orally at a dose of 60 mg/kg. Compounds (3k-m) showed COX-1 and COX-2 inhibitory activity at 0.05 μM.