Boc-PGGG-OCH2Ph | 407629-42-9

• 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-PGGG-OCH2Ph
• 英文别名: Boc-Pro-Gly-Gly-Gly-OCH2Ph；tert-butyl (2S)-2-[[2-oxo-2-[[2-oxo-2-[(2-oxo-2-phenylmethoxyethyl)amino]ethyl]amino]ethyl]carbamoyl]pyrrolidine-1-carboxylate
• CAS: 407629-42-9
• 化学式: C₂₃H₃₂N₄O₇
• 分子量: 476.53
• InChiKey: QUOWXTHHJZSYHE-KRWDZBQOSA-N

物化性质

• 熔点：
  54-55 °C
• 沸点：
  755.3±60.0 °C(Predicted)
• 密度：
  1.247±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  34
• 可旋转键数：
  12
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  143
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  Boc-PGGG-OCH2Ph 在 盐酸 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 作用下， 以 1,4-二氧六环 、 二氯甲烷 为溶剂， 反应 49.0h， 生成 [2-(2-{[1-(2-{2-[2-(2-didecylcarbamoylmethoxyacetylamino)acetylamino]acetylamino}acetyl)pyrrolidine-2-carbonyl]amino}acetylamino)acetylamino]acetic acid benzyl ester
  参考文献：
  名称：

  Replacing proline at the apex of heptapeptide-based chloride ion transporters alters their properties and their ionophoretic efficacy

  摘要：

  一种锚定在膜上的七肽(C18H37)2NHCOCH2OCH2CO–NH–Gly–Gly–Gly–Pro–Gly–Gly–Gly–OCH2Ph已被证明是一种选择性氯阴离子转运体，能够在磷脂双层膜中发挥作用。当Pro被天然氨基酸Leu替换时，活性显著降低。在本研究中，Pro被哌嗪酸（同脯氨酸，Pip）替换，所得到的锚定七肽是一种膜活性的氯选择性转运体。

  DOI：

  10.1039/b206570n
• 作为产物：
  描述：

  BOC-L-脯氨酸 在 palladium on activated charcoal 氢气 、 1-羟基苯并三唑 、 N,N'-二环己基碳二亚胺 作用下， 生成 Boc-PGGG-OCH2Ph
  参考文献：
  名称：

  Pettit, Leslie D.; Steel, Ian; Formicka-Kozlowska, Grazyna, Journal of the Chemical Society, Dalton Transactions, 1985, p. 535 - 540

  摘要：

  DOI：

文献信息

• 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（ ）2N–(Gly)3-Pro-(Gly)3–OCH2Ph或（ ）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。
• [EN] COMPOSITIONS AND METHODS FOR SYNTHETIC AMPHIPHILE-INDUCED CHANGES IN PLANT ROOT MORPHOLOGY<br/>[FR] COMPOSITIONS ET PROCÉDÉS POUR MODIFICATIONS DE MORPHOLOGIE DE RACINES DE PLANTE INDUITES PAR AMPHIPHILE SYNTHÉTIQUE
  申请人：UNIV MISSOURI

  公开号：WO2016022991A1

  公开（公告）日：2016-02-11

  The disclosure provides a method for increasing the lateral root development of a plant by exposing said plant to a composition containing a synthetic amphiphile. By increasing the number of lateral roots, the surface area of the root structure is increased, making the plants better able to survive such stresses as drought or low nutrients

  该公开提供了一种通过将植物暴露在含有合成两性分子的组合物中来增加植物侧根发育的方法。通过增加侧根的数量，根结构的表面积增加，使植物更能够抵抗干旱或低营养等压力。
• Anchor chain length alters the apparent mechanism of chloride channel function in SCMTR derivatives
  作者：Paul H. Schlesinger、Natasha K. Djedovič、Riccardo Ferdani、Jolanta Pajewska、Robert Pajewski、George W. Gokel

  DOI：10.1039/b211629b

  日期：2003.1.23

  Two membrane-anchored heptapeptides have been prepared and their pore-formation behavior in phospholipid bilayer membranes has been found to differ profoundly as a result only of alkyl chain length.

  制备了两个膜锚定的七肽，并发现它们在磷脂双层膜中形成孔洞的行为因仅由烷基链长度不同而存在深刻差异。
• Synthetic ion channels
  申请人：Washington University

  公开号：US20030176641A1

  公开（公告）日：2003-09-18

  The design, synthesis, and characterization of synthetic anion membrane transporters are presented. These novel compounds impart ion permeability to phospholipid bilayers and also modulate cellular volume in mammalian cells in vitro. The compounds insert rapidly into liposomes and planar lipid bilayers.

  介绍了合成阴离子膜转运体的设计、合成和表征。这些新型化合物赋予磷脂双层离子渗透性，并在体外哺乳动物细胞中调节细胞体积。这些化合物能够快速插入到脂质体和平面脂质双层中。
• Cation Dependence of Chloride Ion Complexation by Open-Chained Receptor Molecules in Chloroform Solution
  作者：Robert Pajewski、Riccardo Ferdani、Jolanta Pajewska、Ruiqiong Li、George W. Gokel

  DOI：10.1021/ja0558894

  日期：2005.12.1

  Seventeen peptides, most having the sequence GGGPGGG, but differing in the C- and N-terminal ends, have been studied as anion-complexing agents. These relatively simple, open-chained peptide systems interact with both chloride and the associated cation. Changes, in the N- and C-terminal side chains appear to make little difference in the efficacy of binding. NMR studies suggest that the primary interactions involve amide NH contacts with the chloride anion, and CD spectral analyses suggest a concomitant conformational change upon binding. Changes in binding constants, which are expected in different solvents, also suggest selective solvent interactions with the unbound host that helps to preorganize the open-chained peptide system. Significant differences are apparent in complexation strengths when the heptapeptide chain is shortened or lengthened or when the relative position of proline within the heptapeptide is varied.