7-Bromo-2-methylquinazolin-4-amine | 1432375-67-1

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二氮杂萘
• 英文名称: 7-Bromo-2-methylquinazolin-4-amine
• 英文别名: 7-bromo-2-methylquinazolin-4-amine
• CAS: 1432375-67-1
• 化学式: C₉H₈BrN₃
• 分子量: 238.087
• InChiKey: BITWYWGWWLBGNP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.3
• 重原子数：
  13
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.11
• 拓扑面积：
  51.8
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  tert-butyl ((2S,3R)-3-(tert-butoxy)-1-oxo-1-(3-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)benzenesulfonamido)butan-2-yl)carbamate 、 7-Bromo-2-methylquinazolin-4-amine 在 bis-triphenylphosphine-palladium(II) chloride 、 sodium carbonate 作用下， 以 水 为溶剂， 生成 ((2S,3R)-2-amino-N-((3-(4-amino-2-methylquinazolin-7-yl)phenyl)sulfonyl))-3-hydroxybutanamide
  参考文献：
  名称：

  Identification of Bacteria-Selective Threonyl-tRNA Synthetase Substrate Inhibitors by Structure-Based Design

  摘要：

  A series of potent and bacteria-selective threonyl-tRNA synthetase (ThrRS) inhibitors have been identified using structure-based drug design. These compounds occupied the substrate binding site of ThrRS and showed excellent binding affinities for all of the bacterial orthologues tested. Some of the compounds displayed greatly improved bacterial selectivity. Key residues responsible for potency and bacteria/human ThrRS selectivity have been identified. Antimicrobial activity has been achieved against wild-type Haemophilus influenzae and efflux-deficient mutants of Escherichia coli and Burkholderia thailandensis.

  DOI：

  10.1021/jm301756m

文献信息

• Identification of Bacteria-Selective Threonyl-tRNA Synthetase Substrate Inhibitors by Structure-Based Design
  作者：Min Teng、Mark T. Hilgers、Mark L. Cunningham、Allen Borchardt、Jeffrey B. Locke、Sunny Abraham、Gregory Haley、Bryan P. Kwan、Courtney Hall、Grayson W. Hough、Karen J. Shaw、John Finn

  DOI：10.1021/jm301756m

  日期：2013.2.28

  A series of potent and bacteria-selective threonyl-tRNA synthetase (ThrRS) inhibitors have been identified using structure-based drug design. These compounds occupied the substrate binding site of ThrRS and showed excellent binding affinities for all of the bacterial orthologues tested. Some of the compounds displayed greatly improved bacterial selectivity. Key residues responsible for potency and bacteria/human ThrRS selectivity have been identified. Antimicrobial activity has been achieved against wild-type Haemophilus influenzae and efflux-deficient mutants of Escherichia coli and Burkholderia thailandensis.