(1R)-1-(2-thiophen-2-yl-acetylamino)-1-(3-(2-carboxyvinyl)phenyl)methylboronic acid | 1017233-75-8

• 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: (1R)-1-(2-thiophen-2-yl-acetylamino)-1-(3-(2-carboxyvinyl)phenyl)methylboronic acid
• 英文别名: (1r)-1-(2-Thiophen-2-Yl-Acetylamino)-1-(3-(2-Carboxyvinyl)-Phenyl) Methylboronic Acid；(E)-3-[3-[(R)-borono-[(2-thiophen-2-ylacetyl)amino]methyl]phenyl]prop-2-enoic acid
• CAS: 1017233-75-8
• 化学式: C₁₆H₁₆BNO₅S
• 分子量: 345.184
• InChiKey: ZDYRJUZJSKGVDJ-MOEXGYKKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.26
• 重原子数：
  24
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  135
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  (+)-pinanediol (1R)-1-(2-thiophen-2-yl-acetylamino)-1-(3-(2-methoxycarbonylvinyl)phenyl)methylboronate 在 盐酸 作用下， 反应 1.0h， 以25%的产率得到(1R)-1-(2-thiophen-2-yl-acetylamino)-1-(3-(2-carboxyvinyl)phenyl)methylboronic acid
  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

文献信息

• Structure-based optimization of cephalothin-analogue boronic acids as β-lactamase inhibitors
  作者：Stefania Morandi、Federica Morandi、Emilia Caselli、Brian K. Shoichet、Fabio Prati

  DOI：10.1016/j.bmc.2007.10.075

  日期：2008.2.1

  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.