125096-72-2

Usage

Uses

Used in Pharmaceutical Industry:
8-bromo-4-chloroquinazoline is used as a pharmaceutical intermediate for its potential role in the development of new drugs. Its unique chemical structure and biological activities contribute to its potential use in the synthesis of compounds with therapeutic benefits.
Used in Medicinal Chemistry Research:
8-bromo-4-chloroquinazoline is utilized as a research compound for exploring its antitumor and anti-inflammatory properties. Its study aids in understanding the mechanisms of action and potential applications in treating various diseases and conditions.
Used in Agrochemical Compounds Synthesis:
8-bromo-4-chloroquinazoline is employed as a building block in the synthesis of agrochemical compounds, potentially contributing to the development of new pesticides or other agricultural chemicals that can improve crop protection and yield.
Used in Drug Development:
8-bromo-4-chloroquinazoline is used as a starting material in drug development, where its chemical properties and biological activities are leveraged to create novel therapeutic agents with potential applications in treating a range of diseases, including cancer and inflammatory conditions.

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

Upstream product

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

Relevant academic research and scientific papers

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.

Benzoaromatic heterocyclic compound and application thereof

The invention discloses a benzo aromatic heterocyclic compound and application thereof. The benzo aromatic heterocyclic compound has a structural formula shown in the specification and has remarkable inhibitory activity on a PD-1/PD-L1 signal channel.

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.