n-nonylguanidinium sulphate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机硫酸及其衍生物
• 英文名称: n-nonylguanidinium sulphate
• 英文别名: 2-Nonylguanidine;sulfuric acid；2-nonylguanidine;sulfuric acid
• 化学式: 2C₁₀H₂₃N₃*H₂O₄S
• 分子量: 468.705
• InChiKey: NYBGABIMQRRNMW-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.36
• 重原子数：
  18
• 可旋转键数：
  8
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.9
• 拓扑面积：
  147
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  壬胺 、 S-甲基异硫脲硫酸盐 以 乙醇 为溶剂， 反应 18.0h， 以45%的产率得到n-nonylguanidinium sulphate
  参考文献：
  名称：

  I 2 -Imidazoline Binding Site Affinity of a Structurally Different Type of Ligands

  摘要：

  Two families of compounds with affinity towards the I-2 imidazoline binding sites are reported. The first is a family of compounds structurally related to agmatine with two guanidine or 2-aminoimidazoline groups at each end of an aliphatic chain of six, eight, nine or 12 methylene groups. Second, and following the model of clonidine, we propose another family of compounds also with two guanidine or 2-aminoimidazoline groups at each end of a chain consisting of two phenyl rings connected by groups such as CH2, CO, NH and SO2, The affinity of the compounds towards the I-2 imidazoline binding sites was then evaluated in human brain tissues. In order to determine their pharmacological selectivity versus alpha(2)-adrenoceptors. the affinity for these receptors was also evaluated for the compounds with the highest affinities at I-2 imidazoline binding sites. The results obtained show that many of the compounds exhibit a considerable affinity towards the I-2 imidazoline binding sites. The aliphatic derivatives, in particular, present a very interesting selectivity for the I-2 imidazoline binding sites versus the alpha(2) adrenoceptors. To better understand these findings, mono-guanidinium analogues of the aliphatic derivatives were synthesised and tested showing poor affinity for I-2 imidazoline binding sites. The importance of these results lies in the novelty of the chemical structures studied (dicationic aliphatic compounds particularly) because they are significantly different to those of the I-2 imidazoline binding site ligands reported to date. (C) 2002 Published by Elsevier Science Ltd.

  DOI：

  10.1016/s0968-0896(01)00420-5

文献信息

• US4147804A
  申请人：——

  公开号：US4147804A

  公开（公告）日：1979-04-03
• I 2 -Imidazoline Binding Site Affinity of a Structurally Different Type of Ligands
  作者：Christophe Dardonville、Isabel Rozas、Luis F Callado、J.Javier Meana

  DOI：10.1016/s0968-0896(01)00420-5

  日期：2002.5

  Two families of compounds with affinity towards the I-2 imidazoline binding sites are reported. The first is a family of compounds structurally related to agmatine with two guanidine or 2-aminoimidazoline groups at each end of an aliphatic chain of six, eight, nine or 12 methylene groups. Second, and following the model of clonidine, we propose another family of compounds also with two guanidine or 2-aminoimidazoline groups at each end of a chain consisting of two phenyl rings connected by groups such as CH2, CO, NH and SO2, The affinity of the compounds towards the I-2 imidazoline binding sites was then evaluated in human brain tissues. In order to determine their pharmacological selectivity versus alpha(2)-adrenoceptors. the affinity for these receptors was also evaluated for the compounds with the highest affinities at I-2 imidazoline binding sites. The results obtained show that many of the compounds exhibit a considerable affinity towards the I-2 imidazoline binding sites. The aliphatic derivatives, in particular, present a very interesting selectivity for the I-2 imidazoline binding sites versus the alpha(2) adrenoceptors. To better understand these findings, mono-guanidinium analogues of the aliphatic derivatives were synthesised and tested showing poor affinity for I-2 imidazoline binding sites. The importance of these results lies in the novelty of the chemical structures studied (dicationic aliphatic compounds particularly) because they are significantly different to those of the I-2 imidazoline binding site ligands reported to date. (C) 2002 Published by Elsevier Science Ltd.