125096-72-2

Basic information

• Product Name: 8-bromo-4-chloroquinazoline
• Synonyms: 8-bromo-4-chloroquinazoline;8-broMo-4-chloro-4a,8a-dihydroquinazoline;8-bromo-4-chloroquizoline
• CAS NO: 125096-72-2
• Molecular Formula: C8H4BrClN2
• Molecular Weight: 243.49
• Product Categories: CHIRAL CHEMICALS
• Mol File: 125096-72-2.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 339.695 °C at 760 mmHg
• Flash Point: 159.242 °C
• Appearance: /
• Density: 1.763 g/cm³
• Refractive Index: 1.691
• Storage Temp.: under inert gas (nitrogen or Argon) at 2-8°C
• PKA: -0.27±0.50(Predicted)
• CAS DataBase Reference: 8-bromo-4-chloroquinazoline(CAS DataBase Reference)
• NIST Chemistry Reference: 8-bromo-4-chloroquinazoline(125096-72-2)
• EPA Substance Registry System: 8-bromo-4-chloroquinazoline(125096-72-2)

Safety Data

• Hazardous Substances Data: 125096-72-2(Hazardous Substances Data)

Usage

General Description

8-bromo-4-chloroquinazoline is a chemical compound with the molecular formula C8H4BrClN2. It is a heterocyclic compound with a quinazoline core structure and substituents consisting of a bromine atom at the 8th position and a chlorine atom at the 4th position. 8-bromo-4-chloroquinazoline is of interest in the field of medicinal chemistry as it has been found to possess potential pharmacological activities, including antitumor and anti-inflammatory properties. Additionally, 8-bromo-4-chloroquinazoline has been studied for its potential use as a building block in the synthesis of various pharmaceutical and agrochemical compounds. Its chemical properties and biological activities make it a subject of interest for further research and potential applications in the pharmaceutical industry.

InChI:InChI=1/C8H4BrClN2/c9-6-3-1-2-5-7(6)11-4-12-8(5)10/h1-4H

Upstream product

• 20776-51-6 2-amino-3-bromo benzoic acid 
• 77150-35-7 C₈H₅BrN₂O 

Relevant articles and documents

Discovery of quinazoline derivatives as novel small-molecule inhibitors targeting the programmed cell death-1/programmed cell death-ligand 1 (PD-1/PD-L1) interaction

Development of small molecule PD-1/PD-L1 inhibitors as a novel immunotherapy strategy exhibits great promise. Herein, a novel series of quinazoline derivatives were designed, synthesized and their inhibitory activity against the PD-1/PD-L1 interaction was evaluated through a homogenous time-resolved fluorescence (HTRF) assay. Among them, the compound 39 exhibited the most potent inhibitory activity with an IC50 value of 1.57 nM. Furthermore, the cellular level assays revealed that 39 could inhibit the PD-1/PD-L1 interaction and restore T-cell function, and showed low toxicity on the PBMCs. In addition, the structure-activity relationships (SARs) of the novel quinazoline derivatives were explored and the binding mode of 39 with dimeric PD-L1 was analyzed by molecular docking. This work demonstrates that incorporation of pyrimidine group between the 2 and 3-positions of the biphenyl structure is an effective strategy for designing novel and more potent small molecule PD-1/PD-L1 inhibitors, and 39 can be regarded as a promising lead compound for further investigation.

Rigidification Dramatically Improves Inhibitor Selectivity for RAF Kinases

One effective means to achieve inhibitor specificity for RAF kinases, an important family of cancer drug targets, has been to target the monomeric inactive state conformation of the kinase domain, which, unlike most other kinases, can accommodate sulfonamide-containing drugs such as vemurafenib and dabrafenib because of the presence of a unique pocket specific to inactive RAF kinases. We previously reported an alternate strategy whereby rigidification of a nonselective pyrazolo[3,4-d]pyrimidine-based inhibitor through ring closure afforded moderate but appreciable increases in selectivity for RAF kinases. Here, we show that a further application of the rigidification strategy to a different pyrazolopyrimidine-based scaffold dramatically improved selectivity for RAF kinases. Crystal structure analysis confirmed our inhibitor design hypothesis revealing that 2l engages an active-like state conformation of BRAF normally associated with poorly discriminating inhibitors. When screened against a panel of distinct cancer cell lines, the optimized inhibitor 2l primarily inhibited the proliferation of the expected BRAFV600E-harboring cell lines consistent with its kinome selectivity profile. These results suggest that rigidification could be a general and powerful strategy for enhancing inhibitor selectivity against protein kinases, which may open up therapeutic opportunities not afforded by other approaches.