Boc-Pro-D-Tyr-Val-Orn-Leu-D-Phe-ONSu | 1053422-05-1

• 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-Pro-D-Tyr-Val-Orn-Leu-D-Phe-ONSu
• 英文别名: Boc-Pro-D-Tyr-Val-Orn-Leu-D-Phe-OSu；tert-butyl (2S)-2-[[(2R)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[(2R)-1-(2,5-dioxopyrrolidin-1-yl)oxy-1-oxo-3-phenylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]carbamoyl]pyrrolidine-1-carboxylate
• CAS: 1053422-05-1
• 化学式: C₄₈H₆₈N₈O₁₂
• 分子量: 949.114
• InChiKey: XQXFMKKLCGAYCB-IVLOSMPVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  68
• 可旋转键数：
  25
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  285
• 氢给体数：
  7
• 氢受体数：
  13

反应信息

• 作为反应物：
  描述：

  Boc-Pro-D-Tyr-Val-Orn-Leu-D-Phe-ONSu 在 吡啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 24.0h， 生成 (S)-Pyrrolidine-2-carboxylic acid [(R)-1-[(S)-1-((3R,6S,9S)-3-benzyl-6-isobutyl-2,5,8-trioxo-1,4,7-triaza-cyclododec-9-ylcarbamoyl)-2-methyl-propylcarbamoyl]-2-(4-hydroxy-phenyl)-ethyl]-amide
  参考文献：
  名称：

  Biomimetic synthesis of a peptide antibiotic, gratisin

  摘要：

  Recently, we reported the direct formation of a peptide antibiotic, gramicidin S (GS), cyclo(-D-Phe-Pro-Val-Orn-Leu-)2, by the dimerization–cyclization of pentapeptide active esters, D-Phe-Pro-Val-Orn-Leu-ONSu (-ONSu: succinimide ester), having the sequence identical with that of the linear precursor pentapeptide in the biosynthesis of GS and no protecting group on the side-chain of the Orn residue. This biomimetic approach has been extended to the synthesis of a peptide antibiotic, gratisin (GR), cyclo(-D-Phe-Pro-D-Tyr-Val-Orn-Leu-)2, isolated from Bacillus brevis Y-33. In the cyclization of six hexapeptide succinimide esters having a Val, Orn, Leu, D-Phe, Pro or D-Tyr residue at each C-terminus, only H-D-Phe-Pro-D-Tyr-Val-Orn-Leu-ONSu gave semi-GR and GR in yields of 31 and 8%, respectively. Other hexapeptide esters did not give semi-GR and GR. In both biomimetic syntheses of GS and GR, the amino acid sequences having a Leu residue at the C-terminus are essential. In addition, a change in the concentration of peptide and the polarity of reaction solvents influenced greatly the yields of cyclic monomer (semi-GR) and cyclic dimer (GR). However, the yield of GR by dimerization–cyclization of hexapeptide active ester was lower when compared with the direct formation of GS (38%). The difference may result from differences in the chain length and the configurations of amino acid residues around the Pro residue.

  DOI：

  10.1039/a701537b
• 作为产物：
  描述：

  N-羟基丁二酰亚胺 、 Boc-Pro-D-Tyr-Val-Orn-Leu-D-Phe-OH 在 WSCD*HCl 作用下， 生成 Boc-Pro-D-Tyr-Val-Orn-Leu-D-Phe-ONSu
  参考文献：
  名称：

  Biomimetic synthesis of a peptide antibiotic, gratisin

  摘要：

  Recently, we reported the direct formation of a peptide antibiotic, gramicidin S (GS), cyclo(-D-Phe-Pro-Val-Orn-Leu-)2, by the dimerization–cyclization of pentapeptide active esters, D-Phe-Pro-Val-Orn-Leu-ONSu (-ONSu: succinimide ester), having the sequence identical with that of the linear precursor pentapeptide in the biosynthesis of GS and no protecting group on the side-chain of the Orn residue. This biomimetic approach has been extended to the synthesis of a peptide antibiotic, gratisin (GR), cyclo(-D-Phe-Pro-D-Tyr-Val-Orn-Leu-)2, isolated from Bacillus brevis Y-33. In the cyclization of six hexapeptide succinimide esters having a Val, Orn, Leu, D-Phe, Pro or D-Tyr residue at each C-terminus, only H-D-Phe-Pro-D-Tyr-Val-Orn-Leu-ONSu gave semi-GR and GR in yields of 31 and 8%, respectively. Other hexapeptide esters did not give semi-GR and GR. In both biomimetic syntheses of GS and GR, the amino acid sequences having a Leu residue at the C-terminus are essential. In addition, a change in the concentration of peptide and the polarity of reaction solvents influenced greatly the yields of cyclic monomer (semi-GR) and cyclic dimer (GR). However, the yield of GR by dimerization–cyclization of hexapeptide active ester was lower when compared with the direct formation of GS (38%). The difference may result from differences in the chain length and the configurations of amino acid residues around the Pro residue.

  DOI：

  10.1039/a701537b