1-(5,5-dimethyl-1,3-dioxan-2-yl)ethanone | 71006-65-0

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二恶烷
• 英文名称: 1-(5,5-dimethyl-1,3-dioxan-2-yl)ethanone
• 英文别名: 1-(5,5-Dimethyl-1,3-dioxan-2-yl)ethan-1-one
• CAS: 71006-65-0
• 化学式: C₈H₁₄O₃
• 分子量: 158.197
• InChiKey: HEHWDXVAFUFHNP-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.8
• 重原子数：
  11
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  35.5
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  1-(5,5-dimethyl-1,3-dioxan-2-yl)ethanone 在 4-二甲氨基吡啶 、 sodium ethanolate 、 三乙胺 作用下， 以 乙醇 、 二氯甲烷 为溶剂， 反应 22.17h， 生成 3-butyryl-6-(5,5-dimethyl-1,3-dioxan-2-yl)-6-methyldihydro-2H-pyran-2,4(3H)-dione
  参考文献：
  名称：

  Binding Inhibitors of the Bacterial Sliding Clamp by Design

  摘要：

  The bacterial replisome is a target for the development of new antibiotics to combat drug resistant strains. The beta(2) sliding clamp is an essential component of the replicative machinery, providing a platform for recruitment and function of other replisomal components and ensuring polymerase processivity during DNA replication and repair. A single binding region of the clamp is utilized by its binding partners, which all contain conserved binding motifs. The C-terminal Leu and Phe residues of these motifs are integral to the binding interaction. We acquired three-dimensional structural information on the binding site in beta(2) by a study of the binding of modified peptides. Development of a three-dimensional pharmacophore based on the C-terminal dipeptide of the motif enabled identification of compounds that on further development inhibited alpha-beta(2) interaction at low micromolar concentrations. We report the crystal structure of the complex containing one of these inhibitors, a biphenyl oxime, bound to beta(2), as a starting point for further inhibitor design.

  DOI：

  10.1021/jm2004333

文献信息

• Binding Inhibitors of the Bacterial Sliding Clamp by Design
  作者：Gene Wijffels、Wynona M. Johnson、Aaron J. Oakley、Kathleen Turner、V. Chandana Epa、Susan J. Briscoe、Mitchell Polley、Andris J. Liepa、Albert Hofmann、Jens Buchardt、Caspar Christensen、Pavel Prosselkov、Brian P. Dalrymple、Paul F. Alewood、Philip A. Jennings、Nicholas E. Dixon、David A. Winkler

  DOI：10.1021/jm2004333

  日期：2011.7.14

  The bacterial replisome is a target for the development of new antibiotics to combat drug resistant strains. The beta(2) sliding clamp is an essential component of the replicative machinery, providing a platform for recruitment and function of other replisomal components and ensuring polymerase processivity during DNA replication and repair. A single binding region of the clamp is utilized by its binding partners, which all contain conserved binding motifs. The C-terminal Leu and Phe residues of these motifs are integral to the binding interaction. We acquired three-dimensional structural information on the binding site in beta(2) by a study of the binding of modified peptides. Development of a three-dimensional pharmacophore based on the C-terminal dipeptide of the motif enabled identification of compounds that on further development inhibited alpha-beta(2) interaction at low micromolar concentrations. We report the crystal structure of the complex containing one of these inhibitors, a biphenyl oxime, bound to beta(2), as a starting point for further inhibitor design.