| 1093348-41-4

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 直链 1,3-二芳基丙烷
• CAS: 1093348-41-4
• 化学式: C₁₀₂H₁₅₆N₆O₂₄S₂
• 分子量: 1914.52
• InChiKey: DBGRWXXSIRGRFV-OMBLSHKESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  15.35
• 重原子数：
  134.0
• 可旋转键数：
  75.0
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  354.52
• 氢给体数：
  4.0
• 氢受体数：
  26.0

反应信息

• 作为产物：
  描述：

  (1R)-3-(3,4-dimethoxyphenyl)-1-[3-(4-nitrophenoxycarbonylmethoxy)phenyl]propyl (2S)-1-(3,3-dimethyl-2-oxovaleryl)-piperidine-2-carboxylate 、 bis{10-[(11-amino-3,6,9-trioxaundecanyl)carbamoyl]undecanyl} disulfide bis(trifluoroacetate) 在 吡啶 作用下， 以 二氯甲烷 为溶剂， 反应 7.0h， 以21%的产率得到
  参考文献：
  名称：

  Efficient one-cycle affinity selection of binding proteins or peptides specific for a small-molecule using a T7 phage display pool

  摘要：

  Here, we report an efficient one-cycle affinity selection using a natural-protein or random-peptide T7 phage pool for identification of binding proteins or peptides specific for small-molecules. The screening procedure involved a cuvette type 27-MHz quartz-crystal microbalance (QCM) apparatus with introduction of self-assembled monolayer (SAM) for a specific small-molecule immobilization on the gold electrode surface of a sensor chip. Using this apparatus, we attempted an affinity selection of proteins or peptides against synthetic ligand for FK506-binding protein (SLF) or irinotecan (Iri, CPT-11). An affinity selection using SLF-SAM and a natural-protein T7 phage pool successfully detected FK506-binding protein 12 (FKBP12)-displaying T7 phage after an interaction time of only 10 min. Extensive exploration of time-consuming wash and/or elution conditions together with several rounds of selection was not required. Furthermore, in the selection using a 15-mer random-peptide T7 phage pool and subsequent analysis utilizing receptor ligand contact (RELIC) software, a subset of SLF-selected peptides clearly pinpointed several amino-acid residues within the binding site of FKBP12. Likewise, a subset of Iri-selected peptides pinpointed part of the positive amino-acid region of residues from the Iri-binding site of the well-known direct targets, acetylcholinesterase (AChE) and carboxylesterase (CE). Our findings demonstrate the effectiveness of this method and general applicability for a wide range of small-molecules. (C) 2008 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2008.09.061