2-(acrylamido)ethyl 2,3,6-tri-O-benzoyl-4-O-(2,3,4,6-tetra-O-benzoyl-β-D-galactopyranosyl)-β-D-glucopyranoside | 1318074-08-6

• 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: 2-(acrylamido)ethyl 2,3,6-tri-O-benzoyl-4-O-(2,3,4,6-tetra-O-benzoyl-β-D-galactopyranosyl)-β-D-glucopyranoside
• 英文别名: 2-(N-acryloylamino)ethyl (2,3,4,6-tetra-O-benzoyl-β-D-galactopyranosyl)-(1->4)-2,3,6-tri-O-benzoyl-β-D-glucopyranoside；[(2R,3R,4S,5R,6R)-4,5-dibenzoyloxy-6-[2-(prop-2-enoylamino)ethoxy]-3-[(2S,3R,4S,5S,6R)-3,4,5-tribenzoyloxy-6-(benzoyloxymethyl)oxan-2-yl]oxyoxan-2-yl]methyl benzoate
• CAS: 1318074-08-6
• 化学式: C₆₆H₅₇NO₁₉
• 分子量: 1168.17
• InChiKey: SPCODTMXSAGXHV-AEBIKVJUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  10.8
• 重原子数：
  86
• 可旋转键数：
  30
• 环数：
  9.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  250
• 氢给体数：
  1
• 氢受体数：
  19

反应信息

• 作为反应物：
  描述：

  2-(acrylamido)ethyl 2,3,6-tri-O-benzoyl-4-O-(2,3,4,6-tetra-O-benzoyl-β-D-galactopyranosyl)-β-D-glucopyranoside 在 sodium methylate 作用下， 以 甲醇 为溶剂， 以92%的产率得到2-acrylaminoethyl lactoside
  参考文献：
  名称：

  Investigating Cell Surface Galectin-Mediated Cross-Linking on Glycoengineered Cells

  摘要：

  The galectin family of glycan-binding proteins is thought to mediate many cellular processes by oligomerizing cell surface glycoproteins and glycolipids into higher-order aggregates. This hypothesis reflects the known oligomeric states of the galectins themselves and their binding properties with multivalent ligands in vitro, but direct evidence of their ability to cross-link ligands on a cell surface is lacking. A major challenge in fundamental studies of galectin ligand interactions is that their natural ligands comprise a heterogeneous collection of glyco-conjugates that share related glycan structures but disparate underlying scaffolds. Consequently, there is no obvious means to selectively monitor the behaviors of natural galectin ligands on live cell surfaces. Here we describe an approach for probing the galectin-induced multimerization of glycoconjugates on cultured cells. Using RAFT polymerization, we synthesized well-defined glycopolymers (GPs) functionalized with galectin-binding glycans along the backbone, a lipid group on one end and a fluorophore on the other. After insertion into live cell membranes, the GPs' fluorescence lifetime and diffusion time were measured in the presence and absence of galectin-1. We observed direct evidence for galectin-1-mediated extended cross-linking on the engineered cells, a phenomenon that was dependent on glycan structure. This platform offers a new approach to exploring the "galectin lattice" hypothesis and to defining galectin ligand specificity in a physiologically relevant context.

  DOI：

  10.1021/ja301694s
• 作为产物：
  描述：

  在 三氟甲磺酸三甲基硅酯 作用下， 以 二氯甲烷 为溶剂， 反应 0.08h， 生成 2-(acrylamido)ethyl 2,3,6-tri-O-benzoyl-4-O-(2,3,4,6-tetra-O-benzoyl-β-D-galactopyranosyl)-β-D-glucopyranoside
  参考文献：
  名称：

  Gold catalyzed glycosidations for the synthesis of sugar acrylate/acrylamide hybrids and their utility

  摘要：

  Propargyl glyco 1,2-orthoesters were exploited for the efficient synthesis of interesting glycomonomers such as glyco-acrylates and acrylamides using gold catalysts. It was observed that propargyl glyco 1,2-orthoesters with hydroxyethyl acrylates gives very good yield of the corresponding glyco-acrylates in a single step in the presence of catalytic amount of gold(III) catalyst; whereas, gold catalyzed glycosidation reaction on hydroxyethyl acrylamides was found to yield the corresponding acrylamidoyl 1,2-orthoester which was then converted to the corresponding glycol-acrylamide in the presence of catalytic amount of TMSOTf. Synthesized glyco-acrylate/acrylamide monomers are shown to undergo thiolate addition as well as free radical polymerization (C) 2011 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.carres.2011.04.018

文献信息

• Gold catalyzed glycosidations for the synthesis of sugar acrylate/acrylamide hybrids and their utility
  作者：Shivaji A. Thadke、Mritunjoy Kar、Sayam Sen Gupta、Srinivas Hotha

  DOI：10.1016/j.carres.2011.04.018

  日期：2011.9

  Propargyl glyco 1,2-orthoesters were exploited for the efficient synthesis of interesting glycomonomers such as glyco-acrylates and acrylamides using gold catalysts. It was observed that propargyl glyco 1,2-orthoesters with hydroxyethyl acrylates gives very good yield of the corresponding glyco-acrylates in a single step in the presence of catalytic amount of gold(III) catalyst; whereas, gold catalyzed glycosidation reaction on hydroxyethyl acrylamides was found to yield the corresponding acrylamidoyl 1,2-orthoester which was then converted to the corresponding glycol-acrylamide in the presence of catalytic amount of TMSOTf. Synthesized glyco-acrylate/acrylamide monomers are shown to undergo thiolate addition as well as free radical polymerization (C) 2011 Elsevier Ltd. All rights reserved.
• Investigating Cell Surface Galectin-Mediated Cross-Linking on Glycoengineered Cells
  作者：Brian Belardi、Geoff P. O’Donoghue、Adam W. Smith、Jay T. Groves、Carolyn R. Bertozzi

  DOI：10.1021/ja301694s

  日期：2012.6.13

  The galectin family of glycan-binding proteins is thought to mediate many cellular processes by oligomerizing cell surface glycoproteins and glycolipids into higher-order aggregates. This hypothesis reflects the known oligomeric states of the galectins themselves and their binding properties with multivalent ligands in vitro, but direct evidence of their ability to cross-link ligands on a cell surface is lacking. A major challenge in fundamental studies of galectin ligand interactions is that their natural ligands comprise a heterogeneous collection of glyco-conjugates that share related glycan structures but disparate underlying scaffolds. Consequently, there is no obvious means to selectively monitor the behaviors of natural galectin ligands on live cell surfaces. Here we describe an approach for probing the galectin-induced multimerization of glycoconjugates on cultured cells. Using RAFT polymerization, we synthesized well-defined glycopolymers (GPs) functionalized with galectin-binding glycans along the backbone, a lipid group on one end and a fluorophore on the other. After insertion into live cell membranes, the GPs' fluorescence lifetime and diffusion time were measured in the presence and absence of galectin-1. We observed direct evidence for galectin-1-mediated extended cross-linking on the engineered cells, a phenomenon that was dependent on glycan structure. This platform offers a new approach to exploring the "galectin lattice" hypothesis and to defining galectin ligand specificity in a physiologically relevant context.