N-((2R,3R)-1,3-dihydroxyoctadecan-2-yl)acetamide | 35301-25-8

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 鞘脂
• 英文名称: N-((2R,3R)-1,3-dihydroxyoctadecan-2-yl)acetamide
• 英文别名: N-((1R,2R)-2-hydroxy-1-hydroxymethyl-heptadecyl)-acetamide；L_S-threo-2-Acetylamino-octadecan-1,3-diol；N-((1R,2R)-2-Hydroxy-1-hydroxymethyl-heptadecyl)-acetamid；N-[(2R,3R)-1,3-dihydroxyoctadecan-2-yl]acetamide
• CAS: 35301-25-8
• 化学式: C₂₀H₄₁NO₃
• 分子量: 343.55
• InChiKey: CRJGESKKUOMBCT-WOJBJXKFSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.1
• 重原子数：
  24
• 可旋转键数：
  17
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.95
• 拓扑面积：
  69.6
• 氢给体数：
  3
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N-((2R,3R)-1,3-dihydroxyoctadecan-2-yl)acetamide 生成 N,O,O-triacetyl-D-threo-C18-dihydrosphingosine
  参考文献：
  名称：

  Synthesis of two pairs of enantiomeric C18-sphingosines

  摘要：

  DOI：

  10.1016/s0040-4039(01)93935-8
• 作为产物：
  描述：

  正十四烷基三苯基溴化膦 在 盐酸 、 正丁基锂 、 氢气 、 二苯二硫醚 作用下， 生成 N-((2R,3R)-1,3-dihydroxyoctadecan-2-yl)acetamide
  参考文献：
  名称：

  Synthesis of two pairs of enantiomeric C18-sphingosines

  摘要：

  DOI：

  10.1016/s0040-4039(01)93935-8

文献信息

• Development of Asymmetric Transfer Hydrogenation with a Bifunctional Oxo-Tethered Ruthenium Catalyst in Flow for the Synthesis of a Ceramide (<scp>d</scp>-<i>erythro</i>-CER[NDS])
  作者：Taichiro Touge、Masahiro Kuwana、Yasuhiro Komatsuki、Shigeru Tanaka、Hideki Nara、Kazuhiko Matsumura、Noboru Sayo、Yoshinobu Kashibuchi、Takao Saito

  DOI：10.1021/acs.oprd.8b00338

  日期：2019.4.19

  development of an efficient synthetic route for an optically active ceramide compound (d-erythro-CER[NDS]) is described. The route proceeds through asymmetric transfer hydrogenation in a pipes-in-series flow reactor with oxo-tethered ruthenium complex-catalyzed dynamic kinetic resolution. This synthesis was accomplished without any expensive reagents, and none of the intermediates required isolation

  一种有效的合成路线的用于光学活性的神经酰胺化合物的开发（d -赤-CER [NDS]）进行说明。该路线是在串联的管式反应器中通过不对称转移氢化进行的，该串联反应器具有羰基连接的钌络合物催化的动态动力学拆分。该合成无需任何昂贵的试剂即可完成，并且无需分离任何中间体。这导致了一个健壮的过程，并已成功地在生产规模上运行。
• Sticht et al., 1972, vol. 8, p. 10,17,22
  作者：Sticht et al.

  DOI：——

  日期：——
• Molecular Interactions and Functional Interference between Vitronectin and Transforming Growth Factor-β
  作者：Michael Schoppet、Triantafyllos Chavakis、Nadia Al-Fakhri、Sandip M Kanse、Klaus T Preissner

  DOI：10.1038/labinvest.3780393

  日期：2002.1

  Different extracellular matrix proteins have been described as binding proteins for growth factors, influencing their storage or presentation towards cellular receptors. The multifunctional adhesive glycoprotein vitronectin (VN), which is found in the circulation and widely distributed throughout different tissues, has been implicated in the regulation of vascular cell functions, and these activities could be related to interactions with various growth factors. In vitro, soluble VN interfered with transforming growth factor-beta (TGF-beta) binding to isolated extracellular matrix and was found to associate with TGF-beta1 and TGF-beta2 as well as with other growth factors such as vascular endothelial growth factor, epidermal growth factor, or basic fibroblast growth factor in a saturable manner. In particular, binding of TGF-beta was maximal for the heparin-binding multimeric isoform of VN, whereas VN in a ternary complex with thrombin and antithrombin or plasma VN exhibited weaker binding. Plasminogen activator inhibitor-1 (PAI-1) or heparin, but not desulfated glycosaminoglycans, interfered with binding of VN to TGF-beta, and soluble PAI-1 was able to dissociate VN-bound TGF-beta. Upon limited plasmin proteolysis of VN, only the fragments comprising the intact aminoterminal portion of VN bound to TGF-beta as did a synthetic peptide (amino acids 43 to 62), indicating that TGF-beta and PAI-1 share common binding site(s) on VN. Although VN did not influence TGF-beta bioactivity for mink lung epithelial cells, TGF-beta dose dependently inhibited both urokinase-receptor as well as alpha(v)-integrin-dependent adhesion to VN. This activity of TGF-beta was reminiscent of the antiadhesive function of PAI-1. In atherosclerotic tissue sections, staining patterns of VN and TGF-beta indicated their colocalization. These findings describe VN as a new binding protein for TGF-beta, whereby specific functions of both factors become modulated by this interaction.