N-Fmoc-Pro-Phe-Pro-OBu^t | 221689-37-8

• 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: N-Fmoc-Pro-Phe-Pro-OBu^t
• 英文别名: Fmoc-Pro-Phe-Pro-OtBu；tert-butyl (2S)-1-[(2S)-2-[[(2S)-1-(9H-fluoren-9-ylmethoxycarbonyl)pyrrolidine-2-carbonyl]amino]-3-phenylpropanoyl]pyrrolidine-2-carboxylate
• CAS: 221689-37-8
• 化学式: C₃₈H₄₃N₃O₆
• 分子量: 637.776
• InChiKey: WVGITQCOYDABNV-ZDCRTTOTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  6.1
• 重原子数：
  47
• 可旋转键数：
  11
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  105
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N-Fmoc-Pro-Phe-Pro-OBu^t 在 三(2-氨基乙基)胺 、 氰基磷酸二乙酯 、 N,N-二异丙基乙胺 作用下， 生成 N-Fmoc-Ile-Ile-Pro-Tyr(OBu^t)-Pro-Phe-Pro-OBu^t
  参考文献：
  名称：

  Antineoplastic Agents. 400. Synthesis of the Indian Ocean Marine Sponge Cyclic Heptapeptide Phakellistatin 2^,1a

  摘要：

  Solution-phase synthesis of the marine sponge constituent phakellistatin 2 (1), cyclo(Tyr-Pro-Phe-Prone-Ile-Pro), was completed using a combination of stepwise coupling and (4 + 3) segment condensation. Use of diethyl phosphorocyanidate for the peptide bond formations gave the linear heptapeptide in 54% yield. Cyclization was achieved in high yields utilizing TBTU (2), BOP-C1 (3), PyBroP (4), and HOAt (5), resulting in 50-65% yields of phakellistatin 2 (1) depending on the method employed. The synthetic cyclic peptide was chemically but not biologically identical with the natural product.

  DOI：

  10.1021/np980168m
• 作为产物：
  描述：

  (9H-fluoren-9-yl)methyl tert-butylpyrrolidine-1,2-dicarboxylate 在 三(2-氨基乙基)胺 、 氰基磷酸二乙酯 、 N,N-二异丙基乙胺 作用下， 生成 N-Fmoc-Pro-Phe-Pro-OBu^t
  参考文献：
  名称：

  Antineoplastic Agents. 400. Synthesis of the Indian Ocean Marine Sponge Cyclic Heptapeptide Phakellistatin 2^,1a

  摘要：

  Solution-phase synthesis of the marine sponge constituent phakellistatin 2 (1), cyclo(Tyr-Pro-Phe-Prone-Ile-Pro), was completed using a combination of stepwise coupling and (4 + 3) segment condensation. Use of diethyl phosphorocyanidate for the peptide bond formations gave the linear heptapeptide in 54% yield. Cyclization was achieved in high yields utilizing TBTU (2), BOP-C1 (3), PyBroP (4), and HOAt (5), resulting in 50-65% yields of phakellistatin 2 (1) depending on the method employed. The synthetic cyclic peptide was chemically but not biologically identical with the natural product.

  DOI：

  10.1021/np980168m

文献信息

• Specific fragmentation of thioxo peptides facilitates the assignment of the thioxylated amino acid
  作者：Thomas Pfeifer、Angelika Schierhorn、Rudolf Friedemann、Mario Jakob、Robert Frank、Mike Schutkowski、Gunter Fischer

  DOI：10.1002/(sici)1096-9888(199711)32:10<1064::aid-jms560>3.0.co;2-7

  日期：1997.11

  Low-energy collision-induced dissociation (CID) product ion spectra of a series of singly protonated thioxo peptides produced by electrospray ionization (ESI) were obtained by triple-quadrupole tandem mass spectrometry. The principal feature of the spectra is a preferential cleavage of the peptide bond succeeding the thioxo peptide moiety. Thus this method provides the possibility of assigning the position of the thioxylated amino acid in oligopeptides resulting from the thioxylation procedure with Lawesson's or a related reagent. At low collision energy, dominant B ions and/or complementary Y '' ions are observed. Higher collision energy yields internal ions that consist of two adjacent amino acids encompassing the thioxo peptide bond. The formation of these internal ions and the elimination of CO from them give evidence for the position of the thioxylated amino acid. There are strong indications of a stabilization of the B and internal ions through the formation of a thiazolone. Fragment ions resulting from the cleavage of the thioxo peptide bond are either completely absent or of very low intensity. (C) by John Wiley & Sons, Ltd.No. of Figures:10 No. of Tables:0 No. of Refs:41.