tert-butyl 3-[[(2R,3R,4S,5R,6S)-6-methoxy-3,4,5-tris(phenylmethoxy)oxan-2-yl]methoxy]propanoate | 1351945-78-2

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: tert-butyl 3-[[(2R,3R,4S,5R,6S)-6-methoxy-3,4,5-tris(phenylmethoxy)oxan-2-yl]methoxy]propanoate
• CAS: 1351945-78-2
• 化学式: C₃₅H₄₄O₈
• 分子量: 592.73
• InChiKey: JUSTULYJPAODRA-WJYBGUOCSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.8
• 重原子数：
  43
• 可旋转键数：
  17
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  81.7
• 氢给体数：
  0
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  tert-butyl 3-[[(2R,3R,4S,5R,6S)-6-methoxy-3,4,5-tris(phenylmethoxy)oxan-2-yl]methoxy]propanoate 在 三氟甲磺酸 、 溶剂黄146 作用下， 反应 5.0h， 生成 6-O-[2-(carboxy)ethyl]-2,3,4-tri-O-benzyl-β-D-glucopyranoside 、 6-O-[2-(carboxy)ethyl]-2,3,4-tri-O-benzyl-α-D-glucopyranoside
  参考文献：
  名称：

  Sugar-based peptidomimetics inhibit amyloid β-peptide aggregation

  摘要：

  Alzheimer's disease is characterized by the oligomerization and amyloid fibril formation of amyloid beta-peptide (A beta). We describe a novel class of small water-soluble A beta binding peptidomimetics based on two hydrophobic Ala-Val and Val-Leu dipeptides linked to a D-glucopyranosyl scaffold through aminoalkyl and carboxyethyl links in C1 and C6 positions. These compounds combine the targeting of hydrophobic recognition interfaces with an original hydrophilic sugar beta-breakage strategy. These molecules were shown, by fluorescence thioflavin-T assays, to dramatically slow down the kinetics of amyloid fibril formation even at a low peptidomimetics to A beta ratio of 0.1:1. Electron microscopy images revealed that the peptidomimetics efficiently reduced the amount of typical amyloid fibrils. NMR saturation transfer difference experiments indicated that these molecules interact with A beta aggregated species through their hydrophobic amino acid residues. This inhibition effect was found to be sequence-specific since these molecules did not alter the kinetics of aggregation of another amyloid peptide, IAPP, involved in type 2 diabetes mellitus. (C) 2011 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2011.10.008
• 作为产物：
  描述：

  甲基-6-O-三苯基甲基-alpha-D-吡喃葡萄糖苷 在 四丁基溴化铵 、 sodium hydride 、 对甲苯磺酸 、 sodium hydroxide 作用下， 以 甲醇 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 4.0h， 生成 tert-butyl 3-[[(2R,3R,4S,5R,6S)-6-methoxy-3,4,5-tris(phenylmethoxy)oxan-2-yl]methoxy]propanoate
  参考文献：
  名称：

  Sugar-based peptidomimetics inhibit amyloid β-peptide aggregation

  摘要：

  Alzheimer's disease is characterized by the oligomerization and amyloid fibril formation of amyloid beta-peptide (A beta). We describe a novel class of small water-soluble A beta binding peptidomimetics based on two hydrophobic Ala-Val and Val-Leu dipeptides linked to a D-glucopyranosyl scaffold through aminoalkyl and carboxyethyl links in C1 and C6 positions. These compounds combine the targeting of hydrophobic recognition interfaces with an original hydrophilic sugar beta-breakage strategy. These molecules were shown, by fluorescence thioflavin-T assays, to dramatically slow down the kinetics of amyloid fibril formation even at a low peptidomimetics to A beta ratio of 0.1:1. Electron microscopy images revealed that the peptidomimetics efficiently reduced the amount of typical amyloid fibrils. NMR saturation transfer difference experiments indicated that these molecules interact with A beta aggregated species through their hydrophobic amino acid residues. This inhibition effect was found to be sequence-specific since these molecules did not alter the kinetics of aggregation of another amyloid peptide, IAPP, involved in type 2 diabetes mellitus. (C) 2011 Elsevier Masson SAS. All rights reserved.

  DOI：

  10.1016/j.ejmech.2011.10.008

文献信息

• Sugar-based peptidomimetics inhibit amyloid β-peptide aggregation
  作者：Bertrand Dorgeret、Lucie Khemtémourian、Isabelle Correia、Jean-Louis Soulier、Olivier Lequin、Sandrine Ongeri

  DOI：10.1016/j.ejmech.2011.10.008

  日期：2011.12

  Alzheimer's disease is characterized by the oligomerization and amyloid fibril formation of amyloid beta-peptide (A beta). We describe a novel class of small water-soluble A beta binding peptidomimetics based on two hydrophobic Ala-Val and Val-Leu dipeptides linked to a D-glucopyranosyl scaffold through aminoalkyl and carboxyethyl links in C1 and C6 positions. These compounds combine the targeting of hydrophobic recognition interfaces with an original hydrophilic sugar beta-breakage strategy. These molecules were shown, by fluorescence thioflavin-T assays, to dramatically slow down the kinetics of amyloid fibril formation even at a low peptidomimetics to A beta ratio of 0.1:1. Electron microscopy images revealed that the peptidomimetics efficiently reduced the amount of typical amyloid fibrils. NMR saturation transfer difference experiments indicated that these molecules interact with A beta aggregated species through their hydrophobic amino acid residues. This inhibition effect was found to be sequence-specific since these molecules did not alter the kinetics of aggregation of another amyloid peptide, IAPP, involved in type 2 diabetes mellitus. (C) 2011 Elsevier Masson SAS. All rights reserved.