(S)-2-((S)-2-{[(R)-1-((S)-2-Amino-3-phenyl-propionyl)-pyrrolidine-2-carbonyl]-amino}-6-tert-butoxycarbonylamino-hexanoylamino)-3-phenyl-propionic acid | 911485-34-2

• 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: (S)-2-((S)-2-{[(R)-1-((S)-2-Amino-3-phenyl-propionyl)-pyrrolidine-2-carbonyl]-amino}-6-tert-butoxycarbonylamino-hexanoylamino)-3-phenyl-propionic acid
• 英文别名: H-Phe-D-Pro-Lys(Boc)-Phe-OH；(2S)-2-[[(2S)-2-[[(2R)-1-[(2S)-2-amino-3-phenylpropanoyl]pyrrolidine-2-carbonyl]amino]-6-[(2-methylpropan-2-yl)oxycarbonylamino]hexanoyl]amino]-3-phenylpropanoic acid
• CAS: 911485-34-2
• 化学式: C₃₄H₄₇N₅O₇
• 分子量: 637.776
• InChiKey: LZVMEVFVHNCQNV-LAJGZZDBSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.3
• 重原子数：
  46
• 可旋转键数：
  17
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  180
• 氢给体数：
  5
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  (S)-2-((S)-2-{[(R)-1-((S)-2-Amino-3-phenyl-propionyl)-pyrrolidine-2-carbonyl]-amino}-6-tert-butoxycarbonylamino-hexanoylamino)-3-phenyl-propionic acid 在 benzotriazol-1-yloxyl-tris-(pyrrolidino)-phosphonium hexafluorophosphate 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 24.0h， 生成 [4-((5S,8S,11S,13aR)-5,8-Dibenzyl-4,7,10,13-tetraoxo-tetradecahydro-3a,6,9,12-tetraaza-cyclopentacyclododecen-11-yl)-butyl]-carbamic acid tert-butyl ester
  参考文献：
  名称：

  β²-Amino Acids in the Design of Conformationally Homogeneous cyclo-Peptide Scaffolds

  摘要：

  Herein, we report studies on the influence of chiral, beta(2)-amino acids in the design of conformationally homogeneous cyclic tetrapeptide scaffolds. The cyclic alpha-tetrapeptide cyclo(-Phe-D-Pro-Lys-Phe-) (1) and its four mixed analogues, having one of the alpha-Phe replaced by either an (S)-or an (R)-beta(2)hPhe residue (i.e., cyclo(-(R)-beta(2)hPhe-D-Pro-Lys-Phe) (2a), cyclo(-(S)-beta(2)hPhe-D-Pro-Lys-Phe-) (2b), cyclo(-Phe-D-Pro-Lys-(R)-beta(2)hPhe-) (3a), and cyclo(- Phe- D- Pro- Lys-( R)-, 2hPhe-) ( 3b)), were all synthesized through solidphase procedures followed by solution- phase cyclization. Initially, all five cyclo- peptides were analyzed by H-1 NMR spectroscopic studies in different solvents and at variable temperatures. Subsequently, a detailed 2D NMR spectroscopic analysis of three of the mixed peptides in water was performed, and the information thus extracted was used as restraints in a computational study on the peptides' conformational preference. An X- ray crystallographic study on the side chain- protected (Boc) 2a revealed the solid- state structure of this peptide. The results presented herein, together with previous literature data on beta(3)-amino acid residues, conclusively demonstrate the potential of beta-amino acids in the design of conformationally homogeneous cyclic peptides that are homologous to peptides with known applications in biomedicinal chemistry and as molecular receptors.

  DOI：

  10.1021/jo060854n
• 作为产物：
  描述：

  Fmoc-L-苯丙氨酸 、 N-alpha-芴甲氧羰基-N-epsilon-叔丁氧羰基-L-赖氨酸 、 Fmoc-D-脯氨酸 生成 (S)-2-((S)-2-{[(R)-1-((S)-2-Amino-3-phenyl-propionyl)-pyrrolidine-2-carbonyl]-amino}-6-tert-butoxycarbonylamino-hexanoylamino)-3-phenyl-propionic acid
  参考文献：
  名称：

  β²-Amino Acids in the Design of Conformationally Homogeneous cyclo-Peptide Scaffolds

  摘要：

  Herein, we report studies on the influence of chiral, beta(2)-amino acids in the design of conformationally homogeneous cyclic tetrapeptide scaffolds. The cyclic alpha-tetrapeptide cyclo(-Phe-D-Pro-Lys-Phe-) (1) and its four mixed analogues, having one of the alpha-Phe replaced by either an (S)-or an (R)-beta(2)hPhe residue (i.e., cyclo(-(R)-beta(2)hPhe-D-Pro-Lys-Phe) (2a), cyclo(-(S)-beta(2)hPhe-D-Pro-Lys-Phe-) (2b), cyclo(-Phe-D-Pro-Lys-(R)-beta(2)hPhe-) (3a), and cyclo(- Phe- D- Pro- Lys-( R)-, 2hPhe-) ( 3b)), were all synthesized through solidphase procedures followed by solution- phase cyclization. Initially, all five cyclo- peptides were analyzed by H-1 NMR spectroscopic studies in different solvents and at variable temperatures. Subsequently, a detailed 2D NMR spectroscopic analysis of three of the mixed peptides in water was performed, and the information thus extracted was used as restraints in a computational study on the peptides' conformational preference. An X- ray crystallographic study on the side chain- protected (Boc) 2a revealed the solid- state structure of this peptide. The results presented herein, together with previous literature data on beta(3)-amino acid residues, conclusively demonstrate the potential of beta-amino acids in the design of conformationally homogeneous cyclic peptides that are homologous to peptides with known applications in biomedicinal chemistry and as molecular receptors.

  DOI：

  10.1021/jo060854n