1-hydroxy-5-(3-indolyl)pentane | 3364-38-3

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 吲哚及其衍生物
• 英文名称: 1-hydroxy-5-(3-indolyl)pentane
• 英文别名: 5-indol-3-yl-pentan-1-ol；3-(5-Hydroxy-pentyl)-indol；5-(1H-indol-3-yl)pentan-1-ol
• CAS: 3364-38-3
• 化学式: C₁₃H₁₇NO
• 分子量: 203.284
• InChiKey: DAMHRDVMNDKEDT-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.1
• 重原子数：
  15
• 可旋转键数：
  5
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  36
• 氢给体数：
  2
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  1-hydroxy-5-(3-indolyl)pentane 在 四溴化碳 、 三苯基膦 作用下， 以 乙醚 为溶剂， 反应 0.25h， 以33%的产率得到1-bromo-5-(3-indolyl)pentane
  参考文献：
  名称：

  Novel bisubstrate analog inhibitors of serotonin N-acetyltransferase: the importance of being neutral

  摘要：

  [GRAPHICS]Linker modified novel bisubstrate analog inhibitors 4-7 for serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AANAT) have been designed and synthesized. Examination of these inhibitors with AANAT in vitro suggested that: (i) linker hydrogen bonding makes only modest contributions to the affinity of bisubstrate analog inhibitors studied; (ii) greater than or equal to four methylene groups between the indole and the coenzyme A (CoASH) moieties are required for a bisubstrate analog inhibitor to achieve strong AANAT inhibition; (iii) the AANAT active site appears not to accommodate positively charged linkers as well as neutral ones; and (iv) substrate amine pK(a) depression may constitute one strategy for AANAT substrate recognition and catalysis. The results reported here have enhanced our understanding of AANAT substrate recognition/catalysis, and are important for novel inhibitor design. Since AANAT belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily, our experimental strategies should find applications for other acetyltransferases. (C) 2003 Elsevier Science (USA). All rights reserved.

  DOI：

  10.1016/s0045-2068(03)00081-6
• 作为产物：
  描述：

  5-indol-3-yl-5-oxo-pentanoic acid 在 lithium aluminium tetrahydride 作用下， 以 四氢呋喃 为溶剂， 生成 1-hydroxy-5-(3-indolyl)pentane
  参考文献：
  名称：

  Novel bisubstrate analog inhibitors of serotonin N-acetyltransferase: the importance of being neutral

  摘要：

  [GRAPHICS]Linker modified novel bisubstrate analog inhibitors 4-7 for serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AANAT) have been designed and synthesized. Examination of these inhibitors with AANAT in vitro suggested that: (i) linker hydrogen bonding makes only modest contributions to the affinity of bisubstrate analog inhibitors studied; (ii) greater than or equal to four methylene groups between the indole and the coenzyme A (CoASH) moieties are required for a bisubstrate analog inhibitor to achieve strong AANAT inhibition; (iii) the AANAT active site appears not to accommodate positively charged linkers as well as neutral ones; and (iv) substrate amine pK(a) depression may constitute one strategy for AANAT substrate recognition and catalysis. The results reported here have enhanced our understanding of AANAT substrate recognition/catalysis, and are important for novel inhibitor design. Since AANAT belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily, our experimental strategies should find applications for other acetyltransferases. (C) 2003 Elsevier Science (USA). All rights reserved.

  DOI：

  10.1016/s0045-2068(03)00081-6

文献信息

• Total Synthesis of (+)‐Alstonlarsine A
  作者：Zorana Ferjancic、Andrej Kukuruzar、Filip Bihelovic

  DOI：10.1002/anie.202210297

  日期：2022.9.26

  An enantioselective total synthesis of alkaloid (+)-alstonlarsine A is reported. The key step is a domino sequence comprising enamine formation and a Diels–Alder reaction. The developed methodology for indole C(2)-H carbenoid insertion enabled closure of the 7-membered ring via intramolecular Horner–Wadsworth–Emmons reaction. This approach allowed for the synthesis of other scaffolds containing an

  报道了生物碱 (+)-alstonlarsine A 的对映选择性全合成。关键步骤是多米诺骨牌序列，包括烯胺形成和 Diels-Alder 反应。开发的吲哚 C(2)-H 类胡萝卜素插入方法通过分子内霍纳-沃兹沃思-埃蒙斯反应实现了 7 元环的闭合。这种方法允许合成其他含有与 6、7 和 8 元环融合的吲哚环的支架。
• Novel bisubstrate analog inhibitors of serotonin N-acetyltransferase: the importance of being neutral
  作者：Weiping Zheng、Philip A Cole

  DOI：10.1016/s0045-2068(03)00081-6

  日期：2003.10

  [GRAPHICS]Linker modified novel bisubstrate analog inhibitors 4-7 for serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AANAT) have been designed and synthesized. Examination of these inhibitors with AANAT in vitro suggested that: (i) linker hydrogen bonding makes only modest contributions to the affinity of bisubstrate analog inhibitors studied; (ii) greater than or equal to four methylene groups between the indole and the coenzyme A (CoASH) moieties are required for a bisubstrate analog inhibitor to achieve strong AANAT inhibition; (iii) the AANAT active site appears not to accommodate positively charged linkers as well as neutral ones; and (iv) substrate amine pK(a) depression may constitute one strategy for AANAT substrate recognition and catalysis. The results reported here have enhanced our understanding of AANAT substrate recognition/catalysis, and are important for novel inhibitor design. Since AANAT belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily, our experimental strategies should find applications for other acetyltransferases. (C) 2003 Elsevier Science (USA). All rights reserved.