p-nitrophenyl 6⁵-O-benzyl-α-maltopentaoside | 115850-12-9

• 分子结构分类: 有机化合物 - 有机氧化合物
• 英文名称: p-nitrophenyl 6⁵-O-benzyl-α-maltopentaoside
• 英文别名: Bn(-6)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a1-4)Glc(a)-O-Ph(4-NO2)；(2R,3R,4S,5S,6R)-2-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-6-[(2R,3S,4R,5R,6R)-4,5-dihydroxy-2-(hydroxymethyl)-6-(4-nitrophenoxy)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-6-(phenylmethoxymethyl)oxane-3,4,5-triol
• CAS: 115850-12-9
• 化学式: C₄₃H₆₁NO₂₈
• 分子量: 1039.95
• InChiKey: DHVZALRRYYJCHL-NWVOMCAWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -7.5
• 重原子数：
  72
• 可旋转键数：
  18
• 环数：
  7.0
• sp3杂化的碳原子比例：
  0.72
• 拓扑面积：
  451
• 氢给体数：
  15
• 氢受体数：
  28

反应信息

• 作为反应物：
  描述：

  p-nitrophenyl 6⁵-O-benzyl-α-maltopentaoside 在 K-phosphate buffer 作用下， 以 水 为溶剂， 反应 12.0h， 生成 6³-O-benzyl β-maltotriose 、 6³-O-benzyl α-maltotriose
  参考文献：
  名称：

  Inhibition of Human α-Amylases By Synthetic 6³-O-Benzyl-and 6³-O-β-D-Galactosyl Maltotrionolactones

  摘要：

  Maltooligosaccharides were transformed into both endo-modified oligosaccharidonolactones as substrate analogue inhibitors for human alpha-amylases. p-Nitrophenyl 6(5)-O-benzyl-alpha-maltopentaoside (1) and p-nitrophenyl 6(5)-O-beta-D-galactosyl-alpha-maltopentaoside (11), which have been synthesized as substrates for human alpha-amylases in serum, were selectively hydrolyzed by specific alpha-amylases to afford 6(3)-O-benzyl maltotriose (8) and 6(3)-O-beta-D-galactosyl maltotriose (10), respectively. Both the modified oligomers were chemically oxidized to 6(3)-O-benzyl maltotrionolactone (6) and 6(3)-O-beta-D-galactosyl maltotrionolactone (7), respectively. Compound 6, which is a strong competitive inhibitor, had K-i values of 2.8 and 9.6 X 10(-6) M for human salivary alpha-amylase (HSA) and human pancreatic alpha-amylase (HPA), respectively. On the other hand, the inhibition activity of 7 was about ten times less than 6. These results indicated that the 6-O-substituted hydrophobic benzyl group enhances the binding with enzymes, whereas the corresponding hydrophilic 6-O-beta-D-galactosyl substituted product weakens binding.

  DOI：

  10.1080/07328309908543988
• 作为产物：
  描述：

  在 molecular sieve 、 二甲胺基甲硼烷 、 sodium methylate 、 对甲苯磺酸 作用下， 以260 mg的产率得到p-nitrophenyl 6⁵-O-benzyl-α-maltopentaoside
  参考文献：
  名称：

  Synthesis of p-nitrophenyl 65-O-benzyl-α-maltopentaoside, a substrate for alpha amylases

  摘要：

  p-Nitrophenyl alpha-maltopentaoside, having a benzyl group on O-6 of the terminal (nonreducing) D-glucosyl group was prepared by use of a reductive ring-opening reaction. Highly regioselective reduction of p-nitrophenyl O-(2,3-di-O-benzoyl-4,6-O-benzylidene-alpha-D-glucopyranosyl)-(1----4)- tris[O-(2,3,6-tri-O-benzoyl-alpha-D-glucopyranosyl)-(1----4)]-2,3,6-tri- O- benzoyl-alpha-D-glucopyranoside by dimethylamine-borane and p-toluenesulfonic acid, followed by debenzoylation, gave p-nitrophenyl O-(6-O-benzyl-alpha-D-glucopyranosyl)-(1----4)-tris[O-alpha-D-glucopyran osyl- (1----4)]-alpha-D-glucopyranoside. An experiment was done on the mode of action of human pancreatic and salivary alpha amylases on this derivative. The compound is suitable as a substrate for the assay of alpha amylase when used with glucoamylase and alpha-D-glucosidase as coupling enzymes.

  DOI：

  10.1016/0008-6215(88)84062-x

文献信息

• Synthesis of p-nitrophenyl 65-O-benzyl-α-maltopentaoside, a substrate for alpha amylases
  作者：Shinji Satomura、Tsutomu Iwata、Yoshitsugu Sakata、Kaoru Omichi、Tokuji Ikenaka

  DOI：10.1016/0008-6215(88)84062-x

  日期：1988.5

  p-Nitrophenyl alpha-maltopentaoside, having a benzyl group on O-6 of the terminal (nonreducing) D-glucosyl group was prepared by use of a reductive ring-opening reaction. Highly regioselective reduction of p-nitrophenyl O-(2,3-di-O-benzoyl-4,6-O-benzylidene-alpha-D-glucopyranosyl)-(1----4)- tris[O-(2,3,6-tri-O-benzoyl-alpha-D-glucopyranosyl)-(1----4)]-2,3,6-tri- O- benzoyl-alpha-D-glucopyranoside by dimethylamine-borane and p-toluenesulfonic acid, followed by debenzoylation, gave p-nitrophenyl O-(6-O-benzyl-alpha-D-glucopyranosyl)-(1----4)-tris[O-alpha-D-glucopyran osyl- (1----4)]-alpha-D-glucopyranoside. An experiment was done on the mode of action of human pancreatic and salivary alpha amylases on this derivative. The compound is suitable as a substrate for the assay of alpha amylase when used with glucoamylase and alpha-D-glucosidase as coupling enzymes.
• Inhibition of Human α-Amylases By Synthetic 6³-<i>O</i>-Benzyl-and 6³-<i>O</i>-β-D-Galactosyl Maltotrionolactones
  作者：Masayasu Takada、Koichi Ogawa、Takeomi Murata、Taichi Usui

  DOI：10.1080/07328309908543988

  日期：1999.1.1

  Maltooligosaccharides were transformed into both endo-modified oligosaccharidonolactones as substrate analogue inhibitors for human alpha-amylases. p-Nitrophenyl 6(5)-O-benzyl-alpha-maltopentaoside (1) and p-nitrophenyl 6(5)-O-beta-D-galactosyl-alpha-maltopentaoside (11), which have been synthesized as substrates for human alpha-amylases in serum, were selectively hydrolyzed by specific alpha-amylases to afford 6(3)-O-benzyl maltotriose (8) and 6(3)-O-beta-D-galactosyl maltotriose (10), respectively. Both the modified oligomers were chemically oxidized to 6(3)-O-benzyl maltotrionolactone (6) and 6(3)-O-beta-D-galactosyl maltotrionolactone (7), respectively. Compound 6, which is a strong competitive inhibitor, had K-i values of 2.8 and 9.6 X 10(-6) M for human salivary alpha-amylase (HSA) and human pancreatic alpha-amylase (HPA), respectively. On the other hand, the inhibition activity of 7 was about ten times less than 6. These results indicated that the 6-O-substituted hydrophobic benzyl group enhances the binding with enzymes, whereas the corresponding hydrophilic 6-O-beta-D-galactosyl substituted product weakens binding.