2-methyl-acrylic acid 1-[2-(3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-ethyl]-1H-[1,2,3]triazol-4-ylmethyl ester | 1001586-83-9

• 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: 2-methyl-acrylic acid 1-[2-(3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-ethyl]-1H-[1,2,3]triazol-4-ylmethyl ester
• 英文别名: [1-[2-[(2S,3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyethyl]triazol-4-yl]methyl 2-methylprop-2-enoate
• CAS: 1001586-83-9
• 化学式: C₁₅H₂₃N₃O₈
• 分子量: 373.363
• InChiKey: UESUUJQFLRJUAD-BIGJJFBESA-N

物化性质

• 沸点：
  615.5±65.0 °C(Predicted)
• 密度：
  1.54±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -2
• 重原子数：
  26
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  156
• 氢给体数：
  4
• 氢受体数：
  10

反应信息

• 作为产物：
  描述：

  2-azidoethyl α-D-mannopyranoside 、 甲基丙烯酸丙炔基酯 在 copper(II) sulfate 、 sodium ascorbate 作用下， 以 甲醇 、 水 为溶剂， 以68%的产率得到2-methyl-acrylic acid 1-[2-(3,4,5-trihydroxy-6-hydroxymethyl-tetrahydro-pyran-2-yloxy)-ethyl]-1H-[1,2,3]triazol-4-ylmethyl ester
  参考文献：
  名称：

  Site-Directed Conjugation of “Clicked” Glycopolymers To Form Glycoprotein Mimics:  Binding to Mammalian Lectin and Induction of Immunological Function

  摘要：

  Synthesis of well-defined neoglycopolymer-protein biohybrid materials and a preliminary study focused on their ability of binding mammalian lectins and inducing immunological function is reported. Crucial intermediates for their preparation are well-defined maleimide-terminated neoglycopolymers (M-n = 8-30 kDa; M-w/M-n = 1.20-1.28) presenting multiple copies of mannose epitope units, obtained by combination of transition-metal-mediated living radical polymerization (TMM LRP) and Huisgen [2+3] cycloaddition. Bovine serum albumin (BSA) was employed as single thiol-containing model protein, and the resulting bioconjugates were purified following two independent protocols and characterized by circular dichroism (CD) spectroscopy, SDS PAGE, and SEC HPLC. The versatility of the synthetic strategy presented in this work was demonstrated by preparing a small library of conjugating glycopolymers that only differ from each other for their relative epitope density were prepared by coclicking of appropriate mixtures of mannopyranoside and galactopyranoside azides to the same polyalkyne scaffold intermediate. Surface plasmon resonance binding studies carried out using recombinant rat mannose-binding lectin (MBL) showed clear and dose-dependent MBL binding to glycopolymer-conjugated BSA. In addition, enzyme-linked immunosorbent assay (ELISA) revealed that the neoglycopolymer-protein materials described in this work possess significantly enhanced capacity to activate complement via the lectin pathway when compared with native unmodified BSA.

  DOI：

  10.1021/ja072999x

文献信息

• Site-Directed Conjugation of “Clicked” Glycopolymers To Form Glycoprotein Mimics:  Binding to Mammalian Lectin and Induction of Immunological Function
  作者：Jin Geng、Giuseppe Mantovani、Lei Tao、Julien Nicolas、Gaojian Chen、Russell Wallis、Daniel A. Mitchell、Benjamin R. G. Johnson、Stephen D. Evans、David M. Haddleton

  DOI：10.1021/ja072999x

  日期：2007.12.1

  Synthesis of well-defined neoglycopolymer-protein biohybrid materials and a preliminary study focused on their ability of binding mammalian lectins and inducing immunological function is reported. Crucial intermediates for their preparation are well-defined maleimide-terminated neoglycopolymers (M-n = 8-30 kDa; M-w/M-n = 1.20-1.28) presenting multiple copies of mannose epitope units, obtained by combination of transition-metal-mediated living radical polymerization (TMM LRP) and Huisgen [2+3] cycloaddition. Bovine serum albumin (BSA) was employed as single thiol-containing model protein, and the resulting bioconjugates were purified following two independent protocols and characterized by circular dichroism (CD) spectroscopy, SDS PAGE, and SEC HPLC. The versatility of the synthetic strategy presented in this work was demonstrated by preparing a small library of conjugating glycopolymers that only differ from each other for their relative epitope density were prepared by coclicking of appropriate mixtures of mannopyranoside and galactopyranoside azides to the same polyalkyne scaffold intermediate. Surface plasmon resonance binding studies carried out using recombinant rat mannose-binding lectin (MBL) showed clear and dose-dependent MBL binding to glycopolymer-conjugated BSA. In addition, enzyme-linked immunosorbent assay (ELISA) revealed that the neoglycopolymer-protein materials described in this work possess significantly enhanced capacity to activate complement via the lectin pathway when compared with native unmodified BSA.