Boc-Leu-Val-Phe-OMe | 78123-60-1

• 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-Leu-Val-Phe-OMe
• 英文别名: methyl (2S)-2-[[(2S)-3-methyl-2-[[(2S)-4-methyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoyl]amino]butanoyl]amino]-3-phenylpropanoate
• CAS: 78123-60-1
• 化学式: C₂₆H₄₁N₃O₆
• 分子量: 491.628
• InChiKey: LGVALJUAGCICTR-ACRUOGEOSA-N

物化性质

• 沸点：
  675.7±55.0 °C(Predicted)
• 密度：
  1.095±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.9
• 重原子数：
  35
• 可旋转键数：
  14
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.62
• 拓扑面积：
  123
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  Boc-Leu-Val-Phe-OMe 在 sodium hydroxide 、 盐酸 作用下， 以 甲醇 、 水 为溶剂， 反应 10.0h， 以70%的产率得到Boc-Leu-Val-Phe-OH
  参考文献：
  名称：

  A peptide based two component white light emitting system

  摘要：

  基于聚合物的两组分白光发射系统已经设计和开发，基于在有机溶剂中将含PDI的肽系统作为受体和含斯蒂尔本的肽系统作为供体的共同组装。

  DOI：

  10.1039/c3cc43371d
• 作为产物：
  描述：

  BOC-L-亮氨酸 在 N,N'-二环己基碳二亚胺 、 sodium hydroxide 作用下， 以 甲醇 、 乙酸乙酯 、 N,N-二甲基甲酰胺 为溶剂， 反应 10.0h， 生成 Boc-Leu-Val-Phe-OMe
  参考文献：
  名称：

  A peptide based two component white light emitting system

  摘要：

  基于聚合物的两组分白光发射系统已经设计和开发，基于在有机溶剂中将含PDI的肽系统作为受体和含斯蒂尔本的肽系统作为供体的共同组装。

  DOI：

  10.1039/c3cc43371d

文献信息

• Synthesis of Sansalvamide A derivatives and their cytotoxicity in the MSS colon cancer cell line HT-29
  作者：Thomas J. Styers、Ahmet Kekec、Rodrigo Rodriguez、Joseph D. Brown、Julia Cajica、Po-Shen Pan、Emily Parry、Chris L. Carroll、Irene Medina、Ricardo Corral、Stephanie Lapera、Katerina Otrubova、Chung-Mao Pan、Kathleen L. McGuire、Shelli R. McAlpine

  DOI：10.1016/j.bmc.2006.04.031

  日期：2006.8

  thirty-six Sansalvamide A derivatives, and their biological activity against colon cancer HT-29 cell line, a microsatellite stable (MSS) colon cancer cell-line. The thirty-six compounds can be divided into three subsets, where the first subset of compounds contains L-amino acids, the second subset contains D-amino acids, and the third subset contains both D- and L-amino acids. Five compounds exhibited

  我们报告了36种SAnSAlvamide A衍生物的合成及其对结肠癌HT-29细胞系（一种微卫星稳定（MSS）结肠癌细胞系）的生物活性。这三十六种化合物可分为三个子集，其中化合物的第一子集包含L-氨基酸，第二个子集包含D-氨基酸，而第三子集包含D-和L-氨基酸。五种化合物表现出出色的抑制活性（抑制率> 75％）。化合物的结构活性关系（SAR）确定了位置2或3上的单个D-氨基酸比SAnSAlvamide A肽的细胞毒性提高了10倍。这项工作强调了残基2和3的重要性以及D-氨基酸在该类化合物的非常规SAR中的作用。
• Regioselective structural and functional mimicry of peptides. Design of hydrolytically-stable cyclic peptidomimetic inhibitors of HIV-1 protease.
  作者：G. Abbenante、D. R. March、D. A. Bergman、P. A. Hunt、B. Garnham、R. J. Dancer、J. L. Martin、D. P. Fairlie

  DOI：10.1021/ja00146a007

  日期：1995.10

  Hydrolytically-stable cyclic mimetics of the tripeptides Leu-Asn-Phe and Phe-Ile-Val were designed and incorporated into peptidic inhibitors, Ac-Leu-Asn-Phe}-CHOHCH2-Pro-Ile-Val-NH2 and Ac-Leu-Val-Phe-CHOHCH2-Phe-Ile-Val}-NH2, of HIV-1 protease. Structural mimicry has been established through molecular modeling and X-ray crystallographic studies of inhibitors bound to HIV-1 protease. Cyclic and acyclic inhibitors had similar conformations that were superimposable and formed similar interactions with the enzyme. Functional mimicry was demonstrated by comparable inhibition of the protease by acyclic and cyclic molecules. Further substitution of the residual acyclic Pro-Ile-Val or Leu-Val-Phe inhibitor components, with Pip-NHtBu or Boc-Phe, respectively, gave hydrolytically stable, water-soluble, lipophilic inhibitors of similar potency. The use of cycles to fix the conformations of amino acid sequences in peptides allows regioselective structural mimicry leading to functional mimicry and also permits localized structure-activity optimization in inhibitors of HIV-1 protease. This approach might be usefully applied to inhibitors of other proteins.
• α-Aminoisobutyric acid modified protected analogues of β-amyloid residue 17–20: a change from sheet to helix
  作者：Debasish Haldar、Michael G.B. Drew、Arindam Banerjee

  DOI：10.1016/j.tet.2006.04.036

  日期：2006.6

  The strong intermolecular interactions mediated by short hydrophobic sequences (e.g., 17-20, -L-Leu-L-Val-L-Phe-L-Phe-) in the middle of A beta are known to play a crucial role in the neuropathology of Alzheimer's disease. FTIR, TEM and Congo red binding studies indicated that a series of L-Ala substituted terminally protected peptides related to the sequence 17-20 of the beta-amyloid peptide, adopted D-sheet conformations. However, the Aib-modified analogues disrupt the D-sheet structure and switch over to a 310 helix with increasing number of Aib residues. X-ray crystallography shed some light on the change from sheet to helix at atomic resolution. (c) 2006 Elsevier Ltd. All rights reserved.