(+)-pinanediol 3-(methoxycarbonylvinyl)phenylboronate | 1017233-78-1

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 肉桂酸及其衍生物
• 英文名称: (+)-pinanediol 3-(methoxycarbonylvinyl)phenylboronate
• CAS: 1017233-78-1
• 化学式: C₂₀H₂₅BO₄
• 分子量: 340.227
• InChiKey: GLBOXSRHFRPJND-AOXMCQISSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.81
• 重原子数：
  25.0
• 可旋转键数：
  3.0
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  44.76
• 氢给体数：
  0.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  (+)-pinanediol 3-(methoxycarbonylvinyl)phenylboronate 、 二氯甲烷 在 正丁基锂 作用下， 以 四氢呋喃 、 正己烷 为溶剂， 反应 6.5h， 生成
  参考文献：
  名称：

  Structure-based optimization of cephalothin-analogue boronic acids as β-lactamase inhibitors

  摘要：

  Boronic acids have proved to be promising selective inhibitors of beta-lactamases, acting as transition state analogues. Starting from a previously described nanomolar inhibitor of AmpC beta-lactamase, three new inhibitors were designed to gain interactions with highly conserved residues, such as Asn343, and to bind more tightly to the enzyme. Among these, one was obtained by stereoselective synthesis and succeeded in placing its anionic group into the carboxylate binding site of the enzyme, as revealed by X-ray crystallography of the complex inhibitor/AmpC. Nevertheless, it failed at improving affinity, when compared to the lead from which it was derived. The origins of this structural and energetic discrepancy are discussed.

  DOI：

  10.1016/j.bmc.2007.10.075
• 作为产物：
  描述：

  (E)-methyl 3-(3-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl)acrylate 、 (1S,2S,3R,5S)-(+)-2,3-蒎烷二醇 以 四氢呋喃 为溶剂， 反应 24.0h， 以100%的产率得到(+)-pinanediol 3-(methoxycarbonylvinyl)phenylboronate
  参考文献：
  名称：

  Structure-based optimization of cephalothin-analogue boronic acids as β-lactamase inhibitors

  摘要：

  Boronic acids have proved to be promising selective inhibitors of beta-lactamases, acting as transition state analogues. Starting from a previously described nanomolar inhibitor of AmpC beta-lactamase, three new inhibitors were designed to gain interactions with highly conserved residues, such as Asn343, and to bind more tightly to the enzyme. Among these, one was obtained by stereoselective synthesis and succeeded in placing its anionic group into the carboxylate binding site of the enzyme, as revealed by X-ray crystallography of the complex inhibitor/AmpC. Nevertheless, it failed at improving affinity, when compared to the lead from which it was derived. The origins of this structural and energetic discrepancy are discussed.

  DOI：

  10.1016/j.bmc.2007.10.075