(S)-N-(2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-phenylpropyl)-N-((allyloxy)carbonyl)glycine | 1588517-31-0

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: (S)-N-(2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-phenylpropyl)-N-((allyloxy)carbonyl)glycine
• 英文别名: 2-[[(2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-phenylpropyl]-prop-2-enoxycarbonylamino]acetic acid
• CAS: 1588517-31-0
• 化学式: C₃₀H₃₀N₂O₆
• 分子量: 514.578
• InChiKey: RIYLGCLQOHLGJQ-QFIPXVFZSA-N

物化性质

• 沸点：
  730.6±60.0 °C(Predicted)
• 密度：
  1.260±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.2
• 重原子数：
  38
• 可旋转键数：
  13
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.23
• 拓扑面积：
  105
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  (S)-N-(2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-phenylpropyl)-N-((allyloxy)carbonyl)glycine 在 N,N-二异丙基乙胺 、 三氟乙酸 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 、 乙腈 为溶剂， 反应 5.5h， 生成
  参考文献：
  名称：

  双环咪唑烷-4-酮衍生物作为强效抗菌剂的开发。

  摘要：

  抗生素耐药性已成为全世界最大的公共卫生问题之一。为了对抗细菌感染，通过模仿宿主防御肽的显着理化特征，开发了一系列具有强效广谱抗菌活性和低耐药率的咪唑烷-4-酮衍生物。这些小分子对革兰氏阴性和革兰氏阳性细菌（包括几种耐多药细菌菌株）均表现出有效的活性。同时，时间-杀灭动力学和耐药性研究表明，最有效的化合物3不仅可以快速消除细菌，而且在 MRSA 中表现出较低的耐药概率。进一步的机理研究表明，3通过分解革兰氏阴性和革兰氏阳性细菌的膜来根除细菌病原体。与 HDPs 相比，它们的分子量小、生产成本低，这些咪唑烷-4-酮化合物可能被开发成新一代的抗生素治疗药物，以对抗新出现的耐药性。

  DOI：

  10.1021/acs.jmedchem.0c00171
• 作为产物：
  描述：

  Fmoc-Phe-H 在 sodium cyanoborohydride 、 N,N-二异丙基乙胺 作用下， 以 甲醇 、 二氯甲烷 为溶剂， 生成 (S)-N-(2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-phenylpropyl)-N-((allyloxy)carbonyl)glycine
  参考文献：
  名称：

  从常见的 γ-AApeptide 构建模块快速获取多类肽模拟物

  摘要：

  在此，我们报告了一种高效的新方法，用于制备理论上能够包含任何功能的 γ-AApeptides；该方法使用一些常见的 N-alloc γ-AApeptide 构建模块。更重要的是，使用相同的方法，也可以很容易地生成带有新型骨架支架的新类肽模拟物。我们的结果不仅证明了这种新合成方法的多功能性，而且强调了由此产生的新型肽模拟物在未来可能会发现离散的生物医学/生物材料应用的可能性。

  DOI：

  10.1002/ejoc.201301841

文献信息

• [EN] METHODS OF SYNTHESIZING Y-AAPEPTIDES, Y-AAPEPTIDE BUILDING BLOCKS, Y-AAPEPTIDE LIBRARIES, AND Y-AAPEPTIDE INHIBITORS OF AB40 AGGREGATES<br/>[FR] PROCÉDÉS DE SYNTHÈSE DE PEPTIDES &Ggr;-AA, D'ÉLÉMENTS CONSTITUTIFS &Ggr;-AA, DE BANQUES DE PEPTIDES &Ggr;-AA, ET D'INHIBITEURS DE TYPE PEPTIDES &Ggr;-AA D'AGRÉGATS A&Bgr;40
  申请人：CAI JIANFENG

  公开号：WO2015031084A1

  公开（公告）日：2015-03-05

  Embodiments of the present disclosure provide for γ-AApeptides, γ-AApeptide building blocks, methods of making γ-AApeptides and libraries of γ-AApeptides, methods of screening the γ-AApeptide libraries for desired peptidomimetic activity, and the like. The present disclosure also provides for γ-AApeptides that are inhibitors of Αβ peptide aggregation, methods of inhibiting and disassembling Αβ peptide aggregation, methods of inhibiting the toxicity of Αβ aggregates towards N2a neuroblasotma cells, as well as methods and compounds for treating Alzheimer's disease.

  本公开涉及的实施例提供了γ-AA肽、γ-AA肽构建模块、制备γ-AA肽的方法以及γ-AA肽库，筛选所述γ-AA肽库以获取所需的肽类模拟活性等。本公开还提供了抑制Αβ肽聚集的γ-AA肽、抑制和解除Αβ肽聚集的方法、抑制Αβ聚集物对N2a神经母细胞毒性的方法以及治疗阿尔茨海默病的方法和化合物。
• Helical Antimicrobial Sulfono-γ-AApeptides
  作者：Yaqiong Li、Haifan Wu、Peng Teng、Ge Bai、Xiaoyang Lin、Xiaobing Zuo、Chuanhai Cao、Jianfeng Cai

  DOI：10.1021/acs.jmedchem.5b00537

  日期：2015.6.11

  Host-defense peptides (HDPs) such as magainin 2 have emerged as potential therapeutic agents combating antibiotic resistance. Inspired by their structures and mechanism of action, herein we report the first example of antimicrobial helical sulfono-gamma-AApeptide foldamers. The lead molecule displays broad-spectrum and potent antimicrobial activity against multi-drug-resistant Gram-positive and Gram-negative bacterial pathogens. Time-kill studies and fluorescence microscopy suggest that sulfono-gamma-AApeptides eradicate bacteria by taking a mode of action analogous to that of HDPs. Clear structurefunction relationships exist in the studied sequences. Longer sequences, presumably adopting more-defined helical structures, are more potent than shorter ones. Interestingly, the sequence with less helical propensity in solution could be more selective than the stronger helix-forming sequences. Moreover, this class of antimicrobial agents are resistant to proteolytic degradation. These results may lead to the development of a new class of antimicrobial foldamers combating emerging antibiotic-resistant pathogens.
• METHODS OF SYNTHESIZING y-AAPEPTIDES, y-AAPEPTIDE BUILDING BLOCKS, y-AAPEPTIDE LIBRARIES, AND y-AAPEPTIDE INHIBITORS OF Ab40 AGGREGATES
  申请人：CAI Jianfeng

  公开号：US20160209422A1

  公开（公告）日：2016-07-21

  Embodiments of the present disclosure provide for γ-AApeptides, γ-AApeptide building blocks, methods of making γ-AApeptides and libraries of γ-AApeptides, methods of screening the γ-AApeptide libraries for desired peptidomimetic activity, and the like. The present disclosure also provides for γ-AApeptides that are inhibitors of Aβ peptide aggregation, methods of inhibiting and disassembling Aβ peptide aggregation, methods of inhibiting the toxicity of Aβ aggregates towards N2a neuroblasotma cells, as well as methods and compounds for treating Alzheimer's disease.
• GAMMA-AA-PEPTIDE STAT3/DNA INHIBITORS AND METHODS OF USE
  申请人：H. Lee Moffitt Cancer Center and Research Institute, Inc.

  公开号：US20170101439A1

  公开（公告）日：2017-04-13

  STAT3 hyperphosphorylation, dimerization and DNA binding are required for its ability to contribute to malignant transformation. As such, STAT3 has been recognized as a promising target for cancer therapy. Although a number of inhibitors of STAT3-STAT3 dimerization have been reported, molecular ligands that prevent interactions between STAT3 and DNA are very rare. The γ-AApeptide-based one-bead-one-compound (OBOC) combinatorial library was used, and identified γ-AApeptides that can selectively inhibit STAT3/DNA interaction and suppress the expression levels of STAT3 target genes in intact cells. The results not only validate γ-AApeptides as novel inhibitors of STAT3 signaling pathway, but also demonstrate that in addition to the SH2 domain, the DNA binding domain of STAT3 is targetable for the development of new generation of anti-cancer therapeutics. This also validates the approach of OBOC combinatorial library for the identification of ligands targeting traditionally recognized “undruggable targets”.