2-[[(2S)-butan-2-yl]-(9H-fluoren-9-ylmethoxycarbonyl)amino]acetic acid | 936242-32-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: 2-[[(2S)-butan-2-yl]-(9H-fluoren-9-ylmethoxycarbonyl)amino]acetic acid
• CAS: 936242-32-9
• 化学式: C₂₁H₂₃NO₄
• 分子量: 353.418
• InChiKey: CBLZSQBXEZEKRQ-AWEZNQCLSA-N

物化性质

• 沸点：
  533.1±29.0 °C(Predicted)
• 密度：
  1?+-.0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  26
• 可旋转键数：
  7
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  66.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-((((9H-fluoren-9-yl)methoxy)carbonyl)(2-(tert-butoxy)ethyl)amino)ethanoic acid 、 2-[[(2S)-butan-2-yl]-(9H-fluoren-9-ylmethoxycarbonyl)amino]acetic acid 、 Fmoc-nleu-oh [Fmoc-n-(异丁基)-甘氨酸] 、 2-((((9H-芴-9-基)甲氧基)羰基)(苄基)氨基)乙酸 、 alkaline earth salt of/the/ methylsulfuric acid 、 alkaline earth salt of/the/ methylsulfuric acid 以31 mg的产率得到HOEt-Gly-N(EtOH)Gly-N(iBu)Gly-N(sBu(S))Gly-Sar-Gly-N(Bn)Gly-N(CH2CONH2)Gly-N(CH2CONH2)Gly-N(CH2CONH2)Gly-ol
  参考文献：
  名称：

  Transformation of the amyloidogenic peptide amylin(20–29) into its corresponding peptoid and retropeptoid: Access to both an amyloid inhibitor and template for self-assembled supramolecular tapes

  摘要：

  The highly amyloidogenic peptide sequence of amylin(20-29) was transformed into its corresponding peptoid and retropeptoid sequences to design a novel class of beta-sheet breaker peptides as amyloid inhibitors. This report describes the synthesis of the chiral peptoid building block of L-isoleucine, the solid phase synthesis of the peptoid and retropeptoid sequences of amylin(20-29), and the structural analysis of these amylin derivatives in solution by infrared spectroscopy, circular dichroism, and transmission electron microscopy. It was found that the peptoid sequence did not form amyloid fibrils or any other secondary structures and was able to inhibit amyloid formation of native amylin(20-29). Although the retropeptoid did not form amyloid fibrils it had only modest amyloid inhibitor properties since supramolecular tapes were formed. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2007.01.042
• 作为产物：
  描述：

  在 palladium on activated charcoal 氢气 、 三乙胺 作用下， 生成 2-[[(2S)-butan-2-yl]-(9H-fluoren-9-ylmethoxycarbonyl)amino]acetic acid
  参考文献：
  名称：

  Transformation of the amyloidogenic peptide amylin(20–29) into its corresponding peptoid and retropeptoid: Access to both an amyloid inhibitor and template for self-assembled supramolecular tapes

  摘要：

  The highly amyloidogenic peptide sequence of amylin(20-29) was transformed into its corresponding peptoid and retropeptoid sequences to design a novel class of beta-sheet breaker peptides as amyloid inhibitors. This report describes the synthesis of the chiral peptoid building block of L-isoleucine, the solid phase synthesis of the peptoid and retropeptoid sequences of amylin(20-29), and the structural analysis of these amylin derivatives in solution by infrared spectroscopy, circular dichroism, and transmission electron microscopy. It was found that the peptoid sequence did not form amyloid fibrils or any other secondary structures and was able to inhibit amyloid formation of native amylin(20-29). Although the retropeptoid did not form amyloid fibrils it had only modest amyloid inhibitor properties since supramolecular tapes were formed. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2007.01.042

文献信息

• Transformation of the amyloidogenic peptide amylin(20–29) into its corresponding peptoid and retropeptoid: Access to both an amyloid inhibitor and template for self-assembled supramolecular tapes
  作者：Ronald C. Elgersma、Gwenn E. Mulder、John A.W. Kruijtzer、George Posthuma、Dirk T.S. Rijkers、Rob M.J. Liskamp

  DOI：10.1016/j.bmcl.2007.01.042

  日期：2007.4

  The highly amyloidogenic peptide sequence of amylin(20-29) was transformed into its corresponding peptoid and retropeptoid sequences to design a novel class of beta-sheet breaker peptides as amyloid inhibitors. This report describes the synthesis of the chiral peptoid building block of L-isoleucine, the solid phase synthesis of the peptoid and retropeptoid sequences of amylin(20-29), and the structural analysis of these amylin derivatives in solution by infrared spectroscopy, circular dichroism, and transmission electron microscopy. It was found that the peptoid sequence did not form amyloid fibrils or any other secondary structures and was able to inhibit amyloid formation of native amylin(20-29). Although the retropeptoid did not form amyloid fibrils it had only modest amyloid inhibitor properties since supramolecular tapes were formed. (c) 2007 Elsevier Ltd. All rights reserved.