n-Butyl 4-O-beta-D-Galactopyranosyl-beta-D-glucopyranoside | 93911-06-9

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: n-Butyl 4-O-beta-D-Galactopyranosyl-beta-D-glucopyranoside
• 英文别名: Gal(b1-4)Glc(b)-O-Bu；(2S,3R,4S,5R,6R)-2-[(2R,3S,4R,5R,6R)-6-butoxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol
• CAS: 93911-06-9；93911-07-0；98302-28-4；109527-16-4；115074-35-6
• 化学式: C₁₆H₃₀O₁₁
• 分子量: 398.408
• InChiKey: YUDSSMIBDHJJOE-FZVFFMNZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.9
• 重原子数：
  27
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  179
• 氢给体数：
  7
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  sialic acid 、 n-Butyl 4-O-beta-D-Galactopyranosyl-beta-D-glucopyranoside 在 α-2,3-sialyltransferase 、 cytidine 5′-triphosphate disodium salt 、 CMP-sialic acid synthetase 、 magnesium chloride 、 1,4-二巯基-2,3-丁二醇 、 alkaline phosphatase 作用下， 生成
  参考文献：
  名称：

  Substrate Recognition of the Membrane-Associated Sialidase NEU3 Requires a Hydrophobic Aglycone

  摘要：

  The human neuraminidases (NEU) consist of a family of four isoforms (NEU1-NEU4). Members of this enzyme family are proposed to have important roles in health and disease through regulation of the composition of cellular sialosides. The NEU3 isoform is a membrane-associated enzyme that cleaves glycolipid substrates. However, few reports have examined the substrate specificity of the enzyme for non-natural substrates. We report here a series of 11 synthetic trisaccharides that feature modifications of the aglycone or the Neu5Ac residue of an octyl beta-sialyllactoside. The time course of substrate cleavage by NEU3 was monitored using an electrospray ionization mass spectrometry assay to obtain relative rates (k(rel)). We observed that NEU3 substrate activity was directly dependent upon the hydrophobicity of the aglycone but had no apparent requirement for features of the ceramide headgroup. We also observed that trisaccharides with incorporated azide groups in the Neu5Ac residue at either C9 or the N5-Ac position were substrates, and in the case of the N5-azidoacetyl derivative, the activity was superior to that of GM3. However, the incorporation of larger aryl groups was tolerated only at C9, but not at N5-Ac. We propose a two-site model for enzyme recognition, requiring interaction at both the Neu5Ac residue and the hydrophobic aglycone.

  DOI：

  10.1021/bi200449j

文献信息

• Preparation for the application of agents in mini-droplets
  申请人：Cevc Gregor

  公开号：US20070042030A1

  公开（公告）日：2007-02-22

  The invention relates to a preparation for the application of agents in the form of minuscule droplets of fluid, in particular provided with membrane-like structures consisting of one or several layers of amphiphilic molecules, or an amphiphilic carrier substance, in particular for transporting the agent into and through natural barriers such as skin and similar materials. The preparation contains a concentration of edge active substances which amounts to up to 99 mol-% of the agent concentration which is required for the induction of droplet solubilization. Such preparations are suitable, for example, for the non-invasive applications of antidiabetics, in particular of insulin. The invention, moreover, relates to the methods for the preparation of such formulations.
• US6165500A
  申请人：——

  公开号：US6165500A

  公开（公告）日：2000-12-26
• Substrate Recognition of the Membrane-Associated Sialidase NEU3 Requires a Hydrophobic Aglycone
  作者：Mahendra S. Sandbhor、Naoto Soya、Amgad Albohy、R. Blake Zheng、Jonathan Cartmell、David R. Bundle、John S. Klassen、Christopher W. Cairo

  DOI：10.1021/bi200449j

  日期：2011.8.16

  The human neuraminidases (NEU) consist of a family of four isoforms (NEU1-NEU4). Members of this enzyme family are proposed to have important roles in health and disease through regulation of the composition of cellular sialosides. The NEU3 isoform is a membrane-associated enzyme that cleaves glycolipid substrates. However, few reports have examined the substrate specificity of the enzyme for non-natural substrates. We report here a series of 11 synthetic trisaccharides that feature modifications of the aglycone or the Neu5Ac residue of an octyl beta-sialyllactoside. The time course of substrate cleavage by NEU3 was monitored using an electrospray ionization mass spectrometry assay to obtain relative rates (k(rel)). We observed that NEU3 substrate activity was directly dependent upon the hydrophobicity of the aglycone but had no apparent requirement for features of the ceramide headgroup. We also observed that trisaccharides with incorporated azide groups in the Neu5Ac residue at either C9 or the N5-Ac position were substrates, and in the case of the N5-azidoacetyl derivative, the activity was superior to that of GM3. However, the incorporation of larger aryl groups was tolerated only at C9, but not at N5-Ac. We propose a two-site model for enzyme recognition, requiring interaction at both the Neu5Ac residue and the hydrophobic aglycone.