1-N-octyl-3-(2,3,4-tri-O-benzyl-α-D-galactopyranosyl)propionamide | 213895-87-5

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: 1-N-octyl-3-(2,3,4-tri-O-benzyl-α-D-galactopyranosyl)propionamide
• 英文别名: 3-[(2R,3S,4R,5S,6R)-6-(hydroxymethyl)-3,4,5-tris(phenylmethoxy)oxan-2-yl]-N-octylpropanamide
• CAS: 213895-87-5
• 化学式: C₃₈H₅₁NO₆
• 分子量: 617.826
• InChiKey: RFBHEHDJPKUZTN-PVFDTRMBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.6
• 重原子数：
  45
• 可旋转键数：
  20
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  86.2
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  1-N-octyl-3-(2,3,4-tri-O-benzyl-α-D-galactopyranosyl)propionamide 在 10percent Pd/C 三氟化硼乙醚 、 氢气 、 溶剂黄146 作用下， 以 乙醇 、 二氯甲烷 为溶剂， 反应 16.0h， 生成 Acetic acid (2R,3R,4R,5R,6R)-3-acetoxy-2-acetoxymethyl-5-hydroxy-6-[(2R,3R,4R,5R,6R)-3,4,5-trihydroxy-6-(2-octylcarbamoyl-ethyl)-tetrahydro-pyran-2-ylmethoxy]-tetrahydro-pyran-4-yl ester
  参考文献：
  名称：

  Differential Carbohydrate Recognition of Two GlcNAc-6-sulfotransferases with Possible Roles in L-Selectin Ligand Biosynthesis

  摘要：

  Two human GlcNAc-6-sulfotransferases, CHST2 and HEC-GlcNAc6ST, have been recently identified as possible contributors to the inflammatory response by virtue of their participation in L-selectin ligand biosynthesis. Selective inhibitors would facilitate their functional elucidation and might provide leads for antiinflammatory therapy. Here we investigate the critical elements of a disaccharide substrate that are required for recognition by CHST2 and HEC-GlcNAc6ST. A panel of disaccharide analogues, bearing modifications to the pyranose rings and aglycon substituents, were synthesized and screened for substrate activity with each enzyme. Both GlcNAc-6-sulfotransferases required the 2-N-acetamido and 4-hydroxyl groups of a terminal GlcNAc residue for conversion to product. Both enzymes tolerated modifications to the reducing terminal pyranose. Key differences in recognition of an amide group in the aglycon substituent were observed, providing the basis for future glycomimetic inhibitor design.

  DOI：

  10.1021/ja001224k
• 作为产物：
  描述：

  3-(2,3,4,6-tetra-O-benzyl-α-D-galactopyranosyl)propanoic acid 在 三氟甲磺酸三甲基硅酯 、 sodium methylate 、 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 反应 15.0h， 生成 1-N-octyl-3-(2,3,4-tri-O-benzyl-α-D-galactopyranosyl)propionamide
  参考文献：
  名称：

  Differential Carbohydrate Recognition of Two GlcNAc-6-sulfotransferases with Possible Roles in L-Selectin Ligand Biosynthesis

  摘要：

  Two human GlcNAc-6-sulfotransferases, CHST2 and HEC-GlcNAc6ST, have been recently identified as possible contributors to the inflammatory response by virtue of their participation in L-selectin ligand biosynthesis. Selective inhibitors would facilitate their functional elucidation and might provide leads for antiinflammatory therapy. Here we investigate the critical elements of a disaccharide substrate that are required for recognition by CHST2 and HEC-GlcNAc6ST. A panel of disaccharide analogues, bearing modifications to the pyranose rings and aglycon substituents, were synthesized and screened for substrate activity with each enzyme. Both GlcNAc-6-sulfotransferases required the 2-N-acetamido and 4-hydroxyl groups of a terminal GlcNAc residue for conversion to product. Both enzymes tolerated modifications to the reducing terminal pyranose. Key differences in recognition of an amide group in the aglycon substituent were observed, providing the basis for future glycomimetic inhibitor design.

  DOI：

  10.1021/ja001224k

文献信息

• Differential Carbohydrate Recognition of Two GlcNAc-6-sulfotransferases with Possible Roles in L-Selectin Ligand Biosynthesis
  作者：Brian N. Cook、Sunil Bhakta、Teresa Biegel、Kendra G. Bowman、Joshua I. Armstrong、Stefan Hemmerich、Carolyn R. Bertozzi

  DOI：10.1021/ja001224k

  日期：2000.9.1

  Two human GlcNAc-6-sulfotransferases, CHST2 and HEC-GlcNAc6ST, have been recently identified as possible contributors to the inflammatory response by virtue of their participation in L-selectin ligand biosynthesis. Selective inhibitors would facilitate their functional elucidation and might provide leads for antiinflammatory therapy. Here we investigate the critical elements of a disaccharide substrate that are required for recognition by CHST2 and HEC-GlcNAc6ST. A panel of disaccharide analogues, bearing modifications to the pyranose rings and aglycon substituents, were synthesized and screened for substrate activity with each enzyme. Both GlcNAc-6-sulfotransferases required the 2-N-acetamido and 4-hydroxyl groups of a terminal GlcNAc residue for conversion to product. Both enzymes tolerated modifications to the reducing terminal pyranose. Key differences in recognition of an amide group in the aglycon substituent were observed, providing the basis for future glycomimetic inhibitor design.