[(1S,14S,16R,17R,19R,20S,21S)-19-ethylsulfanyl-1,14-dimethoxy-20-phenylmethoxy-15,18,22-trioxapentacyclo[12.8.0.02,7.08,13.016,21]docosa-2,4,6,8,10,12-hexaen-17-yl]methanol | 647029-85-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 菲及其衍生物
• 英文名称: [(1S,14S,16R,17R,19R,20S,21S)-19-ethylsulfanyl-1,14-dimethoxy-20-phenylmethoxy-15,18,22-trioxapentacyclo[12.8.0.02,7.08,13.016,21]docosa-2,4,6,8,10,12-hexaen-17-yl]methanol
• CAS: 647029-85-4
• 化学式: C₃₁H₃₄O₇S
• 分子量: 550.673
• InChiKey: AGJPTNZFSPIAMF-YCJSCRBWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  39
• 可旋转键数：
  8
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  101
• 氢给体数：
  1
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  [(1S,14S,16R,17R,19R,20S,21S)-19-ethylsulfanyl-1,14-dimethoxy-20-phenylmethoxy-15,18,22-trioxapentacyclo[12.8.0.02,7.08,13.016,21]docosa-2,4,6,8,10,12-hexaen-17-yl]methanol 在 氢氧化钾 、 4 A molecular sieve 、 溴 、 silver carbonate 作用下， 以 四氢呋喃 、 二氯甲烷 、 二甲基亚砜 为溶剂， 生成 [2'-hydroxyethyl]-2-O-benzyl-3,4-O-[9',10'-dimethoxyphenanthrene-9',10'-diyl]-6-O-isobutyl-α-D-mannopyranoside
  参考文献：
  名称：

  Synthesis and Structure−Activity Relationship of Mannose-Based Peptidomimetics Selectively Blocking Integrin α4β7 Binding to Mucosal Addressin Cell Adhesion Molecule-1

  摘要：

  As part of our ongoing research in the development of alpha4beta7 integrin antagonists, we are interested in peptidomimetics based on a rigid scaffold to allow the display of essential side chains in a suitable binding conformation while eliminating backbone amide bonds and therefore improving pharmacokinetic parameters of the drug. Except for a few examples, peptidomimetics scaffolds have only been moderately successful and often yield molecules that lack the potency of their peptide counterparts. However, we present herein a successful application of using a rigid scaffold. Starting from a mannopyranoside analogue previously discovered in our laboratory as an inhibitor of the alpha4beta1/vascular cell adhesion molecule interaction, a biased library of functionalized carbohydrates was developed. One compound emerged from this library as an active and selective antagonist toward the alpha4beta7/mucosal addressin cell adhesion molecule interaction. Conformational. implications and the relevance of different pharmacophoric patterns will be discussed in order to explain the reverse selectivity and enhanced affinity.

  DOI：

  10.1021/jm020487h
• 作为产物：
  描述：

  (8bS,9aR,10S,11R,13R,13aR,14aS)-13-(tert-Butyl-diphenyl-silanyloxymethyl)-11-ethylsulfanyl-8b,14a-dimethoxy-8b,10,11,13,13a,14a-hexahydro-9aH-9,12,14-trioxa-benzo[b]triphenylen-10-ol 在 氢氧化钾 、 四丁基氟化铵 作用下， 以 四氢呋喃 、 二甲基亚砜 为溶剂， 生成 [(1S,14S,16R,17R,19R,20S,21S)-19-ethylsulfanyl-1,14-dimethoxy-20-phenylmethoxy-15,18,22-trioxapentacyclo[12.8.0.02,7.08,13.016,21]docosa-2,4,6,8,10,12-hexaen-17-yl]methanol
  参考文献：
  名称：

  Synthesis and Structure−Activity Relationship of Mannose-Based Peptidomimetics Selectively Blocking Integrin α4β7 Binding to Mucosal Addressin Cell Adhesion Molecule-1

  摘要：

  As part of our ongoing research in the development of alpha4beta7 integrin antagonists, we are interested in peptidomimetics based on a rigid scaffold to allow the display of essential side chains in a suitable binding conformation while eliminating backbone amide bonds and therefore improving pharmacokinetic parameters of the drug. Except for a few examples, peptidomimetics scaffolds have only been moderately successful and often yield molecules that lack the potency of their peptide counterparts. However, we present herein a successful application of using a rigid scaffold. Starting from a mannopyranoside analogue previously discovered in our laboratory as an inhibitor of the alpha4beta1/vascular cell adhesion molecule interaction, a biased library of functionalized carbohydrates was developed. One compound emerged from this library as an active and selective antagonist toward the alpha4beta7/mucosal addressin cell adhesion molecule interaction. Conformational. implications and the relevance of different pharmacophoric patterns will be discussed in order to explain the reverse selectivity and enhanced affinity.

  DOI：

  10.1021/jm020487h

文献信息

• Synthesis and Structure−Activity Relationship of Mannose-Based Peptidomimetics Selectively Blocking Integrin α4β7 Binding to Mucosal Addressin Cell Adhesion Molecule-1
  作者：Elsa Locardi、Jürgen Boer、Armin Modlinger、Anja Schuster、Bernhard Holzmann、Horst Kessler

  DOI：10.1021/jm020487h

  日期：2003.12.1

  As part of our ongoing research in the development of alpha4beta7 integrin antagonists, we are interested in peptidomimetics based on a rigid scaffold to allow the display of essential side chains in a suitable binding conformation while eliminating backbone amide bonds and therefore improving pharmacokinetic parameters of the drug. Except for a few examples, peptidomimetics scaffolds have only been moderately successful and often yield molecules that lack the potency of their peptide counterparts. However, we present herein a successful application of using a rigid scaffold. Starting from a mannopyranoside analogue previously discovered in our laboratory as an inhibitor of the alpha4beta1/vascular cell adhesion molecule interaction, a biased library of functionalized carbohydrates was developed. One compound emerged from this library as an active and selective antagonist toward the alpha4beta7/mucosal addressin cell adhesion molecule interaction. Conformational. implications and the relevance of different pharmacophoric patterns will be discussed in order to explain the reverse selectivity and enhanced affinity.