Boc-Phe-Ac₆c-OMe | 174077-47-5

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: Boc-Phe-Ac₆c-OMe
• 英文别名: Boc-Phe-Ac6c-OMe；methyl 1-[[(2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-phenylpropanoyl]amino]cyclohexane-1-carboxylate
• CAS: 174077-47-5
• 化学式: C₂₂H₃₂N₂O₅
• 分子量: 404.506
• InChiKey: GSWWLFLLQUXBAZ-KRWDZBQOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.8
• 重原子数：
  29
• 可旋转键数：
  9
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  93.7
• 氢给体数：
  2
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  Boc-Phe-Ac₆c-OMe 在 水 、 sodium hydroxide 作用下， 以 甲醇 为溶剂， 反应 10.0h， 生成
  参考文献：
  名称：

  基于三肽的超级有机凝胶剂：结构和功能†

  摘要：

  合成和表征了一系列新颖的基于三肽的低分子量超级有机胶凝剂。研究了在中央氨基酸残基上具有不同空间拥挤的四个三肽。在该系列中，只有位阻较少的肽1和3在不同的饱和烃，原油和芳族溶剂中形成有机凝胶。在柴油中，这些肽以1 wt％的比例形成凝胶，即他们充当超级组织者。有趣的是，两种肽凝胶均显示出高稳定性和显着的自愈特性。由于这些肽具有富电子的苯基系统，因此相应的凝胶还可以与阳离子染料相互作用，并且可以从废水中选择性去除阳离子染料。超级胶凝剂仅从油水两相混合物中固化油具有很高的效率。由于超级胶凝剂在无毒有机溶剂乙醇中的高溶解度，因此该溶液易于处理，只需将乙醇溶液喷洒在油水混合物上，便能够在室温下发挥胶凝作用。可以将有机凝胶下的残留水抽出，并可以通过真空蒸馏从有机凝胶中回收油。因此，超级胶凝剂可以用作低成本，无毒，

  DOI：

  10.1039/c8nj05578e
• 作为产物：
  描述：

  1-氨基-1-环己基甲酸 在 氯化亚砜 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 20.0h， 生成 Boc-Phe-Ac₆c-OMe
  参考文献：
  名称：

  Design and Synthesis of 1-Aminocycloalkane-1-carboxylic Acid-Substituted Deltorphin Analogues:  Unique δ and μ Opioid Activity in Modified Peptides

  摘要：

  Deltorphin analogues were substituted by a series of achiral C-alpha,C-alpha-dialkyl cyclic alpha-amino acids (1-aminocycloalkane-1-carbaxylic acids, Ac(x)c, where (x) = a hexane, pentane, or propane cycloalkane ring) in position 2, 3, 4, or 2 and 3 in deltorphin C, and in position 2 in [Ac(6)(c)2,- des-Phe(3)]deltorphin C hexapeptide. Receptor assays indicated that even though Ac(6)c(2) and Ac(6)c(3) exhibited a diminished K-i delta by ca. 20-fold (2.5-3.3 nM) relative to deltorphin C (K-i delta = 0.15 nM), selectivity was marginally elevated (K-i mu/K-i delta = 1250) or enhanced by about 70%, and both peptides fitted stringent iterative calculations for a two-site binding model (eta = 0.625 and 0.766, respectively, P < 0.0001). The disubstituted [Ac(6)c(2,3)]- or [Ac(6)c(2),des-Phe(3)]deltorphin analogues yielded peptides with decreased K-i delta, such that the latter peptide was essentially inactive. The presence of Ac(5)c or Ac(3)c in place of Phe(3) further diminished K-i delta (15.4 to 19.0 nM), yet delta selectivity only fell about one-half(K-i mu/K-i delta = 440 and 535, respectively), and only the former peptide fitted a two-site binding model (eta = 0.799). The replacement of Asp(4) by Ac(6)c, Ac5c, or Ac(3)c produced essentially nonselective analogues through the acquisition of high mu affinities (2.5, 0.58, and 0.27 nM, respectively) while maintaining high delta affinities (K-i delta = 0.045-0;054 nM) which were about 3 fold greater than that of deltorphin C. Using pharmacological assays in vitro (mouse vas deferens and guinea pig ileum), position 3-substituted analogues all indicated substantial losses in bioactivity, whereas substitution by 1-aminocycloalkanes at the fourth position retained high delta activity. In fact, the bioactivity of [Ac(3)c(4)]deltorphin C indicated a peptide with relatively weak delta selectivity, which was comparable to the observations with the receptor binding data. In summary, the data confirmed that (i) delta selectivity occurs in the absence of D-chirality at position 2, (ii) the aromaticity of Phe(3) is replaceable by an achiral residue with a hydrophobic ring-saturated side chain, and (iii) the acquisition of dual high-affinity analogues occurs through the elimination of the anionic function at position 4 and replacement by an amino acid with a hydrophobic side chain.

  DOI：

  10.1021/jm950490j

文献信息

• Design and Synthesis of 1-Aminocycloalkane-1-carboxylic Acid-Substituted Deltorphin Analogues:  Unique δ and μ Opioid Activity in Modified Peptides
  作者：Angela Breveglieri、Remo Guerrini、Severo Salvadori、Clementina Bianchi、Sharon D. Bryant、Martti Attila、Lawrence H. Lazarus

  DOI：10.1021/jm950490j

  日期：1996.1.1

  Deltorphin analogues were substituted by a series of achiral C-alpha,C-alpha-dialkyl cyclic alpha-amino acids (1-aminocycloalkane-1-carbaxylic acids, Ac(x)c, where (x) = a hexane, pentane, or propane cycloalkane ring) in position 2, 3, 4, or 2 and 3 in deltorphin C, and in position 2 in [Ac(6)(c)2,- des-Phe(3)]deltorphin C hexapeptide. Receptor assays indicated that even though Ac(6)c(2) and Ac(6)c(3) exhibited a diminished K-i delta by ca. 20-fold (2.5-3.3 nM) relative to deltorphin C (K-i delta = 0.15 nM), selectivity was marginally elevated (K-i mu/K-i delta = 1250) or enhanced by about 70%, and both peptides fitted stringent iterative calculations for a two-site binding model (eta = 0.625 and 0.766, respectively, P < 0.0001). The disubstituted [Ac(6)c(2,3)]- or [Ac(6)c(2),des-Phe(3)]deltorphin analogues yielded peptides with decreased K-i delta, such that the latter peptide was essentially inactive. The presence of Ac(5)c or Ac(3)c in place of Phe(3) further diminished K-i delta (15.4 to 19.0 nM), yet delta selectivity only fell about one-half(K-i mu/K-i delta = 440 and 535, respectively), and only the former peptide fitted a two-site binding model (eta = 0.799). The replacement of Asp(4) by Ac(6)c, Ac5c, or Ac(3)c produced essentially nonselective analogues through the acquisition of high mu affinities (2.5, 0.58, and 0.27 nM, respectively) while maintaining high delta affinities (K-i delta = 0.045-0;054 nM) which were about 3 fold greater than that of deltorphin C. Using pharmacological assays in vitro (mouse vas deferens and guinea pig ileum), position 3-substituted analogues all indicated substantial losses in bioactivity, whereas substitution by 1-aminocycloalkanes at the fourth position retained high delta activity. In fact, the bioactivity of [Ac(3)c(4)]deltorphin C indicated a peptide with relatively weak delta selectivity, which was comparable to the observations with the receptor binding data. In summary, the data confirmed that (i) delta selectivity occurs in the absence of D-chirality at position 2, (ii) the aromaticity of Phe(3) is replaceable by an achiral residue with a hydrophobic ring-saturated side chain, and (iii) the acquisition of dual high-affinity analogues occurs through the elimination of the anionic function at position 4 and replacement by an amino acid with a hydrophobic side chain.
• Tripeptide based super-organogelators: structure and function
  作者：Debasish Podder、Srayoshi Roy Chowdhury、Sujay Kumar Nandi、Debasish Haldar

  DOI：10.1039/c8nj05578e

  日期：——

  tripeptide-based low molecular weight super-organogelators were synthesized and characterized. Four tripeptides with diverse steric crowding at the central amino acid residue were studied. From this series, only sterically less hindered peptide 1 and peptide 3 formed organogels in different saturated hydrocarbons, crude oil, and aromatic solvents. In diesel, the peptides formed gels at 1 wt%, i.e. they

  合成和表征了一系列新颖的基于三肽的低分子量超级有机胶凝剂。研究了在中央氨基酸残基上具有不同空间拥挤的四个三肽。在该系列中，只有位阻较少的肽1和3在不同的饱和烃，原油和芳族溶剂中形成有机凝胶。在柴油中，这些肽以1 wt％的比例形成凝胶，即他们充当超级组织者。有趣的是，两种肽凝胶均显示出高稳定性和显着的自愈特性。由于这些肽具有富电子的苯基系统，因此相应的凝胶还可以与阳离子染料相互作用，并且可以从废水中选择性去除阳离子染料。超级胶凝剂仅从油水两相混合物中固化油具有很高的效率。由于超级胶凝剂在无毒有机溶剂乙醇中的高溶解度，因此该溶液易于处理，只需将乙醇溶液喷洒在油水混合物上，便能够在室温下发挥胶凝作用。可以将有机凝胶下的残留水抽出，并可以通过真空蒸馏从有机凝胶中回收油。因此，超级胶凝剂可以用作低成本，无毒，