FMOC-DL-1-氨基茚满-1-羧酸 | 214139-28-3

• 物质功能分类: 生物化工 - 生化试剂 - 氨基酸
• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 中文名称: FMOC-DL-1-氨基茚满-1-羧酸
• 中文别名: 1-(FMOC-氨基)茚满-1-甲酸
• 英文名称: 1-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-2,3-dihydro-1H-indene-1-carboxylic acid
• 英文别名: 1-(9H-fluoren-9-ylmethoxycarbonylamino)-2,3-dihydroindene-1-carboxylic acid
• CAS: 214139-28-3
• 化学式: C₂₅H₂₁NO₄
• 分子量: 399.446
• InChiKey: JKVSMORCWJVCAE-UHFFFAOYSA-N

物化性质

• 熔点：
  180-185°C
• 沸点：
  641.6±54.0 °C(Predicted)
• 密度：
  1.37±0.1 g/cm3(Predicted)
• 稳定性/保质期：
  遵照规定使用和储存，则不会发生分解。

计算性质

• 辛醇/水分配系数(LogP)：
  4.6
• 重原子数：
  30
• 可旋转键数：
  5
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.2
• 拓扑面积：
  75.6
• 氢给体数：
  2
• 氢受体数：
  4

安全信息

• 危险等级：
  IRRITANT
• 海关编码：
  2924299090
• 储存条件：
  存储于-15°C阴凉干燥处

反应信息

• 作为反应物：
  描述：

  苯并噻吩-2-羧酸 、 1,8-二氨基-3,6-二氧杂辛烷 、 Fmoc-L-苯丙氨酸 、 FMOC-DL-1-氨基茚满-1-羧酸 生成 N-[1-[[(2S)-1-[2-[2-(2-aminoethoxy)ethoxy]ethylamino]-1-oxo-3-phenylpropan-2-yl]carbamoyl]-2,3-dihydroinden-1-yl]-1-benzothiophene-2-carboxamide
  参考文献：
  名称：

  α,α-Cyclic aminoacids as useful scaffolds for the preparation of hNK2 receptor antagonists

  摘要：

  MEN 15596 is a small molecule, potent and selective antagonist of NK2 receptor, possessing high affinity and potency at the guinea-pig and human receptors whose pharmacological characterization has been recently published. Here we report how the corresponding class of compounds was derived from a tri-peptide library and the first optimization round to improve both in vitro activity and physicochemical properties. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmcl.2007.06.053
• 作为产物：
  描述：

  1-氨基茚-1-羧酸 、 9-芴甲基-N-琥珀酰亚胺基碳酸酯 在 phosphate buffer 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 24.0h， 生成 FMOC-DL-1-氨基茚满-1-羧酸
  参考文献：
  名称：

  Novel Selective Inhibitors of the Interaction of Individual Nuclear Hormone Receptors with a Mutually Shared Steroid Receptor Coactivator 2

  摘要：

  Nuclear hormone receptor (NR) signaling, currently a therapeutic target in multiple diseases, involves an ordered series of protein interactions to regulate transcription in response to changing hormone levels. Later steps in the process of ligand-dependent signaling are driven by a highly conserved interaction between the NRs and the steroid receptor coactivators (SRCs) that is effected by a conserved interaction motif (L1XXL2L3), known as an NR box. Using computational design and combinatorial chemistry, we have produced novel alpha-helical proteomimetics of the second NR box of SRC2 that exploit structural differences between human estrogen receptor alpha (hERalpha), human estrogen receptor beta (hERbeta), and human thyroid hormone receptor beta (hTRbeta). The resulting library sequentially replaced each leucine with non-natural side chains. Screening this library using a quantitative competition assay revealed compounds that selectively inhibit the interaction of SRC2-2 with each individual NR in preference to its interaction with the other NR. This approach generated highly selective compounds from one that had no specificity for a particular family member. These compounds represent the first family-member-selective competitive inhibitors of the protein interactions of transcription factors.

  DOI：

  10.1021/ja0348391

文献信息

• C-Terminal Modifications of Apelin-13 Significantly Change Ligand Binding, Receptor Signaling, and Hypotensive Action
  作者：Alexandre Murza、Élie Besserer-Offroy、Jérôme Côté、Patrick Bérubé、Jean-Michel Longpré、Robert Dumaine、Olivier Lesur、Mannix Auger-Messier、Richard Leduc、Philippe Sarret、Éric Marsault

  DOI：10.1021/jm501916k

  日期：2015.3.12

  Apelin is the endogenous ligand of the APJ receptor, a member of the G protein-coupled receptor family. This system plays an important role in the regulation of blood pressure and cardiovascular functions. To better understand the role of its C-terminal Phe13 residue on ligand binding, receptor signaling, and hypotension, we report a series of modified analogues in which Phe13 was substituted by unnatural amino acids. These modifications delivered new compounds exhibiting higher affinity and potency to inhibit cAMP accumulation compared to apelin-13. In particular, analogues Bpa(13) or (alpha-Me)Phe(13) were 30-fold more potent to inhibit cAMP accumulation than apelin-13. Tyr(OBn)(13) substitution led to a 60-fold improvement in binding affinity and induced stronger and more sustained drop in blood pressure compared to apelin-13. Our study identified new potent analogues of apelin-13, which represent valuable probes to better understand its structurefunction relationship.
• SYNTHETIC APOLIPOPROTEINS, AND RELATED COMPOSITIONS METHODS AND SYSTEMS FOR NANOLIPOPROTEIN PARTICLES FORMATION
  申请人：LAWRENCE LIVERMORE NATIONAL SECURITY, LLC

  公开号：US20180186860A1

  公开（公告）日：2018-07-05

  Synthetic apolipoproteins based on native/naturally occurring homolog proteins can be prepared using solid-phase peptide synthesis approaches combined with native chemical ligation methods to create analogs of full length apolipoproteins. The chemical synthesis is expected to allow introduction of non-natural amino acids, e.g., α,α′-dialkyl amino acids, with a periodicity that encourages both helix formation and amphipathicity. Such apolipoprotein analogs are expected to encourage, in some embodiments, facile and more complete NLP formation, enabling consideration of full spectrum of nanoparticle-based biotechnology applications ranging from therapeutic sequestration and delivery to energy/biofuel production to biopolymer production.
• Novel Selective Inhibitors of the Interaction of Individual Nuclear Hormone Receptors with a Mutually Shared Steroid Receptor Coactivator 2
  作者：Timothy R. Geistlinger、R. Kiplin Guy

  DOI：10.1021/ja0348391

  日期：2003.6.1

  Nuclear hormone receptor (NR) signaling, currently a therapeutic target in multiple diseases, involves an ordered series of protein interactions to regulate transcription in response to changing hormone levels. Later steps in the process of ligand-dependent signaling are driven by a highly conserved interaction between the NRs and the steroid receptor coactivators (SRCs) that is effected by a conserved interaction motif (L1XXL2L3), known as an NR box. Using computational design and combinatorial chemistry, we have produced novel alpha-helical proteomimetics of the second NR box of SRC2 that exploit structural differences between human estrogen receptor alpha (hERalpha), human estrogen receptor beta (hERbeta), and human thyroid hormone receptor beta (hTRbeta). The resulting library sequentially replaced each leucine with non-natural side chains. Screening this library using a quantitative competition assay revealed compounds that selectively inhibit the interaction of SRC2-2 with each individual NR in preference to its interaction with the other NR. This approach generated highly selective compounds from one that had no specificity for a particular family member. These compounds represent the first family-member-selective competitive inhibitors of the protein interactions of transcription factors.
• α,α-Cyclic aminoacids as useful scaffolds for the preparation of hNK2 receptor antagonists
  作者：Alessandro Sisto、Maria Altamura、Franco Cardinali、Piero D’Andrea、Cristina Rossi、Daniela Fattori

  DOI：10.1016/j.bmcl.2007.06.053

  日期：2007.9

  MEN 15596 is a small molecule, potent and selective antagonist of NK2 receptor, possessing high affinity and potency at the guinea-pig and human receptors whose pharmacological characterization has been recently published. Here we report how the corresponding class of compounds was derived from a tri-peptide library and the first optimization round to improve both in vitro activity and physicochemical properties. (c) 2007 Elsevier Ltd. All rights reserved.