(S)-1-(3,3-二甲基-2-氧代戊酰基)哌啶-2-羧酸乙酯 | 152754-33-1

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 中文名称: (S)-1-(3,3-二甲基-2-氧代戊酰基)哌啶-2-羧酸乙酯
• 英文名称: ethyl (2S)-1-(1,2-dioxo-3,3-dimethylpentyl)-2-piperidinecarboxylate
• 英文别名: (S)-Ethyl 1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate；ethyl (2S)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate
• CAS: 152754-33-1
• 化学式: C₁₅H₂₅NO₄
• 分子量: 283.368
• InChiKey: CAXFSIWSCHLEMR-NSHDSACASA-N

物化性质

• 沸点：
  370.7±52.0 °C(Predicted)
• 密度：
  1.079±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  20
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  63.7
• 氢给体数：
  0
• 氢受体数：
  4

安全信息

• 海关编码：
  2933399090

反应信息

• 作为反应物：
  描述：

  (S)-1-(3,3-二甲基-2-氧代戊酰基)哌啶-2-羧酸乙酯 在 lithium hydroxide 作用下， 以 甲醇 为溶剂， 反应 6.5h， 以80%的产率得到(S)-1-(3,3-二甲基-2-氧戊烷酰基)哌啶-2-羧酸
  参考文献：
  名称：

  Design, synthesis, and kinetic evaluation of high-affinity FKBP ligands and the X-ray crystal structures of their complexes with FKBP12

  摘要：

  The design and synthesis of high-affinity FKBP12 ligands is described. These compounds potently inhibit the cis-trans-peptidylprolyl isomerase (rotamase) activity catalyzed by FKBP12 with inhibition constants (K(i,app)) as low as 1 nM, yet they possess remarkable structural simplicity relative to FK506 and rapamycin, from which they are conceptually derived. The atomic structures of three FKBP12-ligand complexes and of one unbound ligand were determined by X-ray crystallography and are compared to the FKBP12-FK506 and FKBP12-rapamycin complexes.

  DOI：

  10.1021/ja00075a008
• 作为产物：
  描述：

  magnesium,2-methylbutane,chloride 、 (S)-1-(2-甲氧基-2-氧代乙酰基)哌啶-2-羧酸乙酯 以 四氢呋喃 、 乙醚 为溶剂， 反应 3.0h， 以75%的产率得到(S)-1-(3,3-二甲基-2-氧代戊酰基)哌啶-2-羧酸乙酯
  参考文献：
  名称：

  [EN] PROTEASE INHIBITORS
  [FR] INHIBITEURS DES PROTÉASES

  摘要：

  公开号：

  WO2010077317A3

文献信息

• PROTEASE INHIBITORS
  申请人：Mutz Mitchell W.

  公开号：US20120041019A1

  公开（公告）日：2012-02-16

  Compounds useful as protease inhibitors are provided, as are methods of use and preparation of such compounds and compositions containing such compounds. In one embodiment, the compounds are useful for inhibiting HIV protease enzymes, and are therefore useful in slowing the proliferation of HIV.

  本发明提供了一些有用的蛋白酶抑制剂化合物，以及使用和制备这些化合物的方法和含有这些化合物的组合物。在一种实施方式中，这些化合物可用于抑制HIV蛋白酶酶，因此可用于减缓HIV的增殖。
• [EN] PROTEASE INHIBITORS<br/>[FR] INHIBITEURS DES PROTÉASES
  申请人：AMPLYX PHARMACEUTICALS INC

  公开号：WO2010077317A3

  公开（公告）日：2010-10-28
• Design, synthesis, and kinetic evaluation of high-affinity FKBP ligands and the X-ray crystal structures of their complexes with FKBP12
  作者：Dennis A. Holt、Juan I. Luengo、Dennis S. Yamashita、Hye Ja Oh、Arda L. Konialian、Hwa Kwo Yen、Leonard W. Rozamus、Martin Brandt、Mary J. Bossard、Mark A. Levy、Drake S. Eggleston、Jun Liang、L. Wayne Schultz、Thomas J. Stout、Jon Clardy

  DOI：10.1021/ja00075a008

  日期：1993.11.1

  The design and synthesis of high-affinity FKBP12 ligands is described. These compounds potently inhibit the cis-trans-peptidylprolyl isomerase (rotamase) activity catalyzed by FKBP12 with inhibition constants (K(i,app)) as low as 1 nM, yet they possess remarkable structural simplicity relative to FK506 and rapamycin, from which they are conceptually derived. The atomic structures of three FKBP12-ligand complexes and of one unbound ligand were determined by X-ray crystallography and are compared to the FKBP12-FK506 and FKBP12-rapamycin complexes.
• Evaluation of Synthetic FK506 Analogues as Ligands for the FK506-Binding Proteins 51 and 52
  作者：Ranganath Gopalakrishnan、Christian Kozany、Steffen Gaali、Christoph Kress、Bastiaan Hoogeland、Andreas Bracher、Felix Hausch

  DOI：10.1021/jm201746x

  日期：2012.5.10

  The FK506-binding proteins (FKBP) 51 and 52 are cochaperones that modulate the signal transduction of steroid hormone receptors. Both proteins have been implicated in prostate cancer. Furthermore, single nucleotide polymorphisms in the gene encoding FKBP51 have been associated with a variety of psychiatric disorders. Rapamycin and FK506 are two macrocyclic natural products that bind to these proteins indiscriminately but with nanomolar affinity. We here report the cocrystal structure of FKBP51 with a simplified alpha-ketoamide analogue derived from FK506 and the first structure-activity relationship analysis for FKBP51 and FKBP52 based on this compound. In particular, the tert-pentyl group of this ligand was systematically replaced by a cyclohexyl ring system, which more closely resembles the pyranose ring in the high-affinity ligands rapamycin and FK506. The interaction with FKBPs was found to be surprisingly tolerant to the stereochemistry of the attached cyclohexyl substituents. The molecular basis for this tolerance was elucidated by X-ray cocrystallography.