(5S-aminomethyl-2,2-dimethyl-[1,3]dioxolan-4S-ylmethyl)carbamic acid 9H-fluoren-9-ylmethyl ester | 675606-43-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: (5S-aminomethyl-2,2-dimethyl-[1,3]dioxolan-4S-ylmethyl)carbamic acid 9H-fluoren-9-ylmethyl ester
• 英文别名: 9H-fluoren-9-ylmethyl N-[[(4S,5S)-5-(aminomethyl)-2,2-dimethyl-1,3-dioxolan-4-yl]methyl]carbamate
• CAS: 675606-43-6
• 化学式: C₂₂H₂₆N₂O₄
• 分子量: 382.459
• InChiKey: OEPOFHPFBPVJLK-PMACEKPBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  28
• 可旋转键数：
  6
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.41
• 拓扑面积：
  82.8
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  (5S-aminomethyl-2,2-dimethyl-[1,3]dioxolan-4S-ylmethyl)carbamic acid 9H-fluoren-9-ylmethyl ester 在 N,N-二异丙基乙胺 、 bromo-tris(1-pyrrolidinyl)phosphonium hexafluorophosphate 、 三氟乙酸 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 22.0h， 生成 N-[4-(9H-fluoren-9ylmethoxycarbonylamino)-2S,3S-dihydroxybutyl]-2R,3R-dihydroxysuccinamic acid benzyl ester
  参考文献：
  名称：

  Design and synthesis of novel hydrophilic spacers for the reduction of nonspecific binding proteins on affinity resins

  摘要：

  Tubulin and actin often bind nonspecifically to affinity chromatography resins, complicating research toward identifying the cellular targets. Reduction of nonspecific binding proteins is important for success in finding such targets. We herein disclose the design, synthesis, and effectiveness in reduction of nonspecific binding proteins, of novel hydrophilic spacers (2-5), which were introduced between matrices and a ligand. Among them, tartaric acid derivative (5) exhibited the most effective reduction of nonspecific binding proteins, whilst maintaining binding of the target protein. Introduction of 5 on TOYOPEARL reduced tubulin and actin by almost 65% and 90% compared to that without the hydrophilic spacer, respectively, with effective binding to the target protein, FKBP12. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2004.03.052
• 作为产物：
  描述：

  9-芴甲基-N-琥珀酰亚胺基碳酸酯 、 (4S,5S)-4,5-二(氨甲基)-2,2-二甲基二氧杂烷 以 四氢呋喃 为溶剂， 反应 0.5h， 以53%的产率得到(5S-aminomethyl-2,2-dimethyl-[1,3]dioxolan-4S-ylmethyl)carbamic acid 9H-fluoren-9-ylmethyl ester
  参考文献：
  名称：

  Design and synthesis of novel hydrophilic spacers for the reduction of nonspecific binding proteins on affinity resins

  摘要：

  Tubulin and actin often bind nonspecifically to affinity chromatography resins, complicating research toward identifying the cellular targets. Reduction of nonspecific binding proteins is important for success in finding such targets. We herein disclose the design, synthesis, and effectiveness in reduction of nonspecific binding proteins, of novel hydrophilic spacers (2-5), which were introduced between matrices and a ligand. Among them, tartaric acid derivative (5) exhibited the most effective reduction of nonspecific binding proteins, whilst maintaining binding of the target protein. Introduction of 5 on TOYOPEARL reduced tubulin and actin by almost 65% and 90% compared to that without the hydrophilic spacer, respectively, with effective binding to the target protein, FKBP12. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2004.03.052

文献信息

• Method of inhibiting nonspecific interaction between molecules on solid phase support
  申请人：Tanaka Akito

  公开号：US20060177943A1

  公开（公告）日：2006-08-10

  The present invention provides a method of suppressing the nonspecific interaction between molecules, characterized in that in a process to immobilize a molecule onto a solid phase carrier and analyze the specific interaction between the molecule and a molecule that specifically interacts with the molecule on the solid phase, the hydrophobic property of the solid phase surface in the solid phase carrier is regulated, particularly a hydrophilic spacer is interlaid at the time of immobilization of the molecule onto the solid phase carrier, which method makes it possible to suppress the nonspecific interaction between the molecules, and to reduce nonspecific adsorption to the solid phase.

  本发明提供了一种抑制分子之间非特异性相互作用的方法，其特征在于在将分子固定到固相载体并分析与固相上特异性相互作用的分子之间的过程中，调节固相载体中固相表面的疏水性质，特别是在将分子固定到固相载体时，交错放置了亲水性间隔物，该方法使得能够抑制分子之间的非特异性相互作用，并减少对固相的非特异性吸附。
• METHOD OF INHIBITING NONSPECIFIC INTERACTION BETWEEN MOLECULES ON SOLID PHASE SUPPORT
  申请人：Reverse Proteomics Research Institute Co., Ltd

  公开号：EP1553412A1

  公开（公告）日：2005-07-13

  The present invention provides a method of suppressing the nonspecific interaction between molecules, characterized in that in a process to immobilize a molecule onto a solid phase carrier and analyze the specific interaction between the molecule and a molecule that specifically interacts with the molecule on the solid phase, the hydrophobic property of the solid phase surface in the solid phase carrier is regulated, particularly a hydrophilic spacer is interlaid at the time of immobilization of the molecule onto the solid phase carrier, which method makes it possible to suppress the nonspecific interaction between the molecules, and to reduce nonspecific adsorption to the solid phase.

  本发明提供了一种抑制分子间非特异性相互作用的方法，其特征在于，在将分子固定在固相载体上并分析该分子与固相上与该分子特异性相互作用的分子之间的特异性相互作用的过程中、调节固相载体中固相表面的疏水性，特别是在将分子固定到固相载体上时，在固相载体中插入亲水间隔物，这种方法可以抑制分子之间的非特异性相互作用，减少对固相的非特异性吸附。
• US7919653B2
  申请人：——

  公开号：US7919653B2

  公开（公告）日：2011-04-05
• Design and synthesis of novel hydrophilic spacers for the reduction of nonspecific binding proteins on affinity resins
  作者：Takaaki Shiyama、Minoru Furuya、Akira Yamazaki、Tomohiro Terada、Akito Tanaka

  DOI：10.1016/j.bmc.2004.03.052

  日期：2004.6

  Tubulin and actin often bind nonspecifically to affinity chromatography resins, complicating research toward identifying the cellular targets. Reduction of nonspecific binding proteins is important for success in finding such targets. We herein disclose the design, synthesis, and effectiveness in reduction of nonspecific binding proteins, of novel hydrophilic spacers (2-5), which were introduced between matrices and a ligand. Among them, tartaric acid derivative (5) exhibited the most effective reduction of nonspecific binding proteins, whilst maintaining binding of the target protein. Introduction of 5 on TOYOPEARL reduced tubulin and actin by almost 65% and 90% compared to that without the hydrophilic spacer, respectively, with effective binding to the target protein, FKBP12. (C) 2004 Elsevier Ltd. All rights reserved.