N,N-dioctadecylterephthalamic acid | 173278-40-5

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: N,N-dioctadecylterephthalamic acid
• 英文别名: N,N-dioctadecylterephtalamic acid；4-(Dioctadecylcarbamoyl)benzoic acid
• CAS: 173278-40-5
• 化学式: C₄₄H₇₉NO₃
• 分子量: 670.116
• InChiKey: JUBJVAGVPUYHFB-UHFFFAOYSA-N

物化性质

• 熔点：
  51-52 °C
• 沸点：
  743.3±43.0 °C(Predicted)
• 密度：
  0.932±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  18.6
• 重原子数：
  48
• 可旋转键数：
  36
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.82
• 拓扑面积：
  57.6
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  N,N-dioctadecylterephthalamic acid 在 palladium on activated charcoal 氰基磷酸二乙酯 、 氢气 、 三乙胺 作用下， 以 四氢呋喃 、 乙醇 为溶剂， 反应 116.08h， 生成 N-[((S)-1-Carbamoyl-3-methyl-butylcarbamoyl)-methyl]-N',N'-dioctadecyl-terephthalamide
  参考文献：
  名称：

  Molecular Recognition of Aqueous Dipeptides at Multiple Hydrogen-Bonding Sites of Mixed Peptide Monolayers

  摘要：

  Oligopeptide amphiphiles with different dipeptide moieties of -XYNH(2) (X = Gly and Ala, Y = Gly, Ala, Val, Leu, and Phe) were synthesized. Binding of aqueous dipeptides onto monolayers of equimolar mixtures of these amphiphiles with a benzoic acid amphiphile (2C(18)BCOOH) was investigated by pi-A isotherm measurement, FT-IR spectroscopy, and XPS elemental analysis. For given GlyX dipeptides (X = neutral and hydrophobic residues), the binding ratio was lessened with increasing sizes of the side chain of the Y residue in the GlyY dipeptide moiety of the host amphiphiles. The Langmuir-type saturation behavior was observed for binding of GlyLeu to an equimolar monolayer of 2C(18)BGly(2)NH(2) and 2C(18)BCOOH. Its binding constant of 475 M(-1) was 10 times larger than that observed for a single-component monolayer of 2C(18)BGly(2)NH(2) (K = 35 M(-1)). The saturation guest/host ratio was 0.47. The mode of substrate insertion into the binding site was examined by FT-IR spectroscopy. When the hydrophobic residue was on the C-terminal of a guest dipeptide (GlyX), the C-terminal insertion was selected with accompanying formation of cyclic carboxylic acid dimers at the interface. In the case of XGly guests, the N-terminal insertion with salt bridge formation with the host was observed. When the two residues of a dipeptide had close hydrophobicities, both C- and N-terminal insertions were observed. Formation of these binding sites is apparently induced by dipeptide binding.

  DOI：

  10.1021/ja961526f
• 作为产物：
  描述：

  双十八烷基胺 、 对苯二甲酸 在 氯化亚砜 、 三乙胺 作用下， 以 甲苯 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.67h， 以37%的产率得到N,N-dioctadecylterephthalamic acid
  参考文献：
  名称：

  The effect of midpolar regime mimics on anion transport mediated by amphiphilic heptapeptides

  摘要：

  合成了九种两亲性庚肽，即合成阴离子转运蛋白（SATs），其形式为（C18H37）2N–Y–(Gly)3-Pro-(Gly)3–OCH2Ph。单位（OH2）Y代表二酸，即琥珀酸、戊二酸、二甘醇酸、3-硫代戊二酸、N-甲基亚氨基二甘氨酸、间苯二甲酸和对苯二甲酸。此外，Y可以不存在或以醋酸形式存在，形成结构（C18H37）2N–(Gly)3-Pro-(Gly)3–OCH2Ph或（C18H37）2N–(Gly)4-Pro-(Gly)3–OCH2Ph。曾报道过二甘醇酸衍生物，但其余化合物是新的。这九种肽以不同的效力介导DOPC/DOPA囊泡中Cl–的释放。含有Y的两亲性庚肽的氯离子释放顺序为戊二酸、琥珀酸 > 3-硫代戊二酸 > 对苯二甲酸 > 醋酸，N-甲基亚氨基二醋酸，> 无Y，间苯二甲酸。Cl–的释放通常随时间呈指数衰减，但对于更具柔韧性的二酸，曲线形状明显呈S形。进行了计算研究以评估构象差异。总的来说，对于那些能够在脯氨酸N末端侧形成线性构象的SATs，氯离子释放与二酸的极性最为相关。

  DOI：

  10.1039/b705179b

文献信息

• Molecular Recognition of Aqueous Dipeptides by Noncovalently Aligned Oligoglycine Units at the Air/Water Interface
  作者：Xiao Cha、Katsuhiko Ariga、Mitsuhiko Onda、Toyoki Kunitake

  DOI：10.1021/ja00153a003

  日期：1995.12

  promoted by hydrophobic interaction. The binding was not detected when either of the terephthaloyl and glycylglycinamide units were absent in the monolayer component. Dipeptides with the C-terminal glycine residue (X'Gly) were not bound at all. These results are satisfied by a molecular model in which guest peptides were inserted into the monolayer from the C-terminal. The observed binding selectivity

  摘要：通过 nA 等温线测量和 FT-IR 光谱研究了水性二肽 GlyX 和 X'Gly（X = Leu、Phe、Pro 和 Ala；X' = Leu 和 Phe）与二烷基低聚甘氨酰两亲物的单层的结合, 和 XPS 元素分析。具有 N 端甘氨酸残基 (GlyX) 的二肽被选择性地结合到两亲物的单层上，其中双十八胺部分通过对苯二酰单元与甘氨酰甘氨酰胺头部基团连接。当亚相中的二肽 (GlyLeu) 浓度变化时，观察到 Langmuir 型饱和行为，等摩尔结合和 35 MI 的结合常数。结合效率按GlyPhe>GlyLeu>GlyPro>GlyAla的顺序增加，表明结合是由疏水相互作用促进的。当单层组分中不存在对苯二甲酰和甘氨酰甘氨酰胺单元中的任何一个时，未检测到结合。具有 C 端甘氨酸残基 (X'Gly) 的二肽根本没有结合。这些结果被一个分子模型所满足，其中客体肽从 C 端插入单层。观察到的结合选择性是通过
• US4642375A
  申请人：——

  公开号：US4642375A

  公开（公告）日：1987-02-10
• The effect of midpolar regime mimics on anion transport mediated by amphiphilic heptapeptides
  作者：Robert Pajewski、Jolanta Pajewska、Ruiqiong Li、Megan M. Daschbach、Elizabeth A. Fowler、George W. Gokel

  DOI：10.1039/b705179b

  日期：——

  Nine amphiphilic heptapeptides, synthetic anion transporters (SATs) of the form (C18H37)2N–Y–(Gly)3-Pro-(Gly)3–OCH2Ph were prepared. The unit (OH2)Y represents the diacids succinic, glutaric, diglycolic, 3-thiaglutaric, N-methyliminodiglycine, isophthalic, and terephthalic acids. Additionally, Y was absent or present as acetic acid affording the structure (C18H37)2N–(Gly)3-Pro-(Gly)3–OCH2Ph or (C18H37)2N–(Gly)4-Pro-(Gly)3–OCH2Ph. The diglycolic acid derivative was reported previously but the remaining compounds are new. These nine peptides mediated release of Cl– from DOPC/DOPA vesicles with varying efficacy. Chloride release diminished for the Y-containing amphiphilic heptapeptides in the order glutaric, succinic > 3-thiaglutaric > terephthalic > acetic, N-methyliminodiacetic, > no Y, isophthalic. The release of Cl– was generally exponential over time but the curve shapes were distinctly sigmoidal for the more flexible diacids. Computational studies were undertaken to assess differences in conformation. Overall, it appeared that Cl– release for those SATs that could adopt a linear conformation on the N-terminal side of proline correlated best with the polarity of the diacid.

  合成了九种两亲性庚肽，即合成阴离子转运蛋白（SATs），其形式为（C18H37）2N–Y–(Gly)3-Pro-(Gly)3–OCH2Ph。单位（OH2）Y代表二酸，即琥珀酸、戊二酸、二甘醇酸、3-硫代戊二酸、N-甲基亚氨基二甘氨酸、间苯二甲酸和对苯二甲酸。此外，Y可以不存在或以醋酸形式存在，形成结构（C18H37）2N–(Gly)3-Pro-(Gly)3–OCH2Ph或（C18H37）2N–(Gly)4-Pro-(Gly)3–OCH2Ph。曾报道过二甘醇酸衍生物，但其余化合物是新的。这九种肽以不同的效力介导DOPC/DOPA囊泡中Cl–的释放。含有Y的两亲性庚肽的氯离子释放顺序为戊二酸、琥珀酸 > 3-硫代戊二酸 > 对苯二甲酸 > 醋酸，N-甲基亚氨基二醋酸，> 无Y，间苯二甲酸。Cl–的释放通常随时间呈指数衰减，但对于更具柔韧性的二酸，曲线形状明显呈S形。进行了计算研究以评估构象差异。总的来说，对于那些能够在脯氨酸N末端侧形成线性构象的SATs，氯离子释放与二酸的极性最为相关。
• Molecular Recognition of Aqueous Dipeptides at Multiple Hydrogen-Bonding Sites of Mixed Peptide Monolayers
  作者：Xiao Cha、Katsuhiko Ariga、Toyoki Kunitake

  DOI：10.1021/ja961526f

  日期：1996.1.1

  Oligopeptide amphiphiles with different dipeptide moieties of -XYNH(2) (X = Gly and Ala, Y = Gly, Ala, Val, Leu, and Phe) were synthesized. Binding of aqueous dipeptides onto monolayers of equimolar mixtures of these amphiphiles with a benzoic acid amphiphile (2C(18)BCOOH) was investigated by pi-A isotherm measurement, FT-IR spectroscopy, and XPS elemental analysis. For given GlyX dipeptides (X = neutral and hydrophobic residues), the binding ratio was lessened with increasing sizes of the side chain of the Y residue in the GlyY dipeptide moiety of the host amphiphiles. The Langmuir-type saturation behavior was observed for binding of GlyLeu to an equimolar monolayer of 2C(18)BGly(2)NH(2) and 2C(18)BCOOH. Its binding constant of 475 M(-1) was 10 times larger than that observed for a single-component monolayer of 2C(18)BGly(2)NH(2) (K = 35 M(-1)). The saturation guest/host ratio was 0.47. The mode of substrate insertion into the binding site was examined by FT-IR spectroscopy. When the hydrophobic residue was on the C-terminal of a guest dipeptide (GlyX), the C-terminal insertion was selected with accompanying formation of cyclic carboxylic acid dimers at the interface. In the case of XGly guests, the N-terminal insertion with salt bridge formation with the host was observed. When the two residues of a dipeptide had close hydrophobicities, both C- and N-terminal insertions were observed. Formation of these binding sites is apparently induced by dipeptide binding.