L-arginyl-L-tryptophyl-L-arginine benzylamide | 1016644-01-1

• 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: L-arginyl-L-tryptophyl-L-arginine benzylamide
• 英文别名: R-W-R-NHBn；RWR-NHBn；RWRNHBn；H-Arg-Trp-Arg-NHBn；(2S)-2-amino-N-[(2S)-1-[[(2S)-1-(benzylamino)-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]-5-(diaminomethylideneamino)pentanamide
• CAS: 1016644-01-1
• 化学式: C₃₀H₄₃N₁₁O₃
• 分子量: 605.743
• InChiKey: HMRLQEZRHQRGFB-HVCNVCAESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.5
• 重原子数：
  44
• 可旋转键数：
  17
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.37
• 拓扑面积：
  258
• 氢给体数：
  9
• 氢受体数：
  6

反应信息

• 作为产物：
  描述：

  苄胺 、 Fmoc-L-色氨酸(Boc)-OH 、 Fmoc-Pbf-L-精氨酸 在 aminomethyl-terminated Tentagel resin 、 sodium cyanoborohydride 、 1-羟基苯并三唑 、 4-(4-甲酰基-3,5-二甲氧基苯氧基)-丁酸 、 N,N'-二异丙基碳二亚胺 、 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 甲醇 、 N,N-二甲基甲酰胺 为溶剂， 反应 0.67h， 生成 L-arginyl-L-tryptophyl-L-arginine benzylamide
  参考文献：
  名称：

  In Vitro Characterization of Human Peptide Transporter hPEPT1 Interactions and Passive Permeation Studies of Short Cationic Antimicrobial Peptides

  摘要：

  The present study assesses the permeation of cationic antimicrobial di- and tripeptides derived from lactoferricin via interaction with the human intestinal peptide transporter hPEPT1 and via passive routes. While some tested peptides displayed moderate affinity (0.6 and 2.7 mM) for interaction with hPEPT1, none served as substrate for hPEPT1 expressed by Xenopus laevis oocytes. It is shown that structural strategies employed to generate sufficient biological activity and metabolic stability such as introduction of large hydrophobic unnatural amino acids and different C-terminal modifications counteracted hPEPT1 mediated uptake. Most of the included peptides were nevertheless shown to permeate at rates suggesting moderate to excellent human oral absorption in the applied phospholipid vesicle-based passive permeation assay. Although the main factor governing passive permeation appears to be the hydrophobicity, peptide structure was also important and the overall permeation behavior was difficult to predict. Comparisons with a theoretical prediction model were also performed.

  DOI：

  10.1021/jm1015704