H-Asp-Tyr-D-Phe-Gly-Trp-N(Me)Nle-Asp-Phe-NH2

• 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: H-Asp-Tyr-D-Phe-Gly-Trp-N(Me)Nle-Asp-Phe-NH2
• 英文别名: (3S)-3-amino-4-[[(2S)-1-[[(2R)-1-[[2-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-1-oxohexan-2-yl]-methylamino]-3-(1H-indol-3-yl)-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-1-oxo-3-phenylpropan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-4-oxobutanoic acid
• 化学式: C₅₅H₆₆N₁₀O₁₃
• 分子量: 1075.19
• InChiKey: IJHCWGDIGBABKC-GDHOWUIUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.2
• 重原子数：
  78
• 可旋转键数：
  30
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  375
• 氢给体数：
  12
• 氢受体数：
  14

反应信息

• 作为产物：
  描述：

  Boc-L-天冬氨酸 4-苄酯 、 Boc-O-苄基-L-酪氨酸 、 Boc-D-苯丙氨酸 、 N-叔丁氧羰基-L-色氨酸 、 alkaline earth salt of/the/ methylsulfuric acid 生成 H-Asp-Tyr-D-Phe-Gly-Trp-N(Me)Nle-Asp-Phe-NH2
  参考文献：
  名称：

  The Use of Topographical Constraints In Receptor Mapping:  Investigation of the Topographical Requirements of the Tryptophan 30 Residue for Receptor Binding of Asp-Tyr-d-Phe-Gly-Trp-(N-Me)Nle-Asp-Phe-NH₂ (SNF 9007), a Cholecystokinin (26−33) Analogue That Binds to both CCK-B and δ-Opioid Receptors

  摘要：

  The cholecystokinin (26-33) [CCK(26-33)] octapeptide analog Asp-Tyr-D-Phe-Gly-Trp(N-Me)-Nle-Asp-Phe-NH2 (SNF 9007) is a potent and selective ligand for both the CCK-B and delta-opioid receptors. Pharmacological studies of SNF 9007 suggest a relationship between the ligand requirements of CCK-B and delta-opioid receptors, which further implies a possible structural relationship between these receptors. We have utilized topographical constrainment of the important Trp(30) residue to investigate structural features of SNF 9007 that would distinguish between binding requirements in this region for the CCK-B and delta-opioid receptors, Thus, the four optically pure isomers of beta-MeTrp were substituted for L-Trp(30) Of SNF 9007. Receptor binding results suggest that the preferred topography of the Trp(30) residue for CCK-B receptor binding may be the 2S,3S (erythro-L) configuration whereas for the delta-opioid receptor it may be the 2S,3R (threo-L) configuration. Molecular modeling studies of these ligands further support the recently revised receptor-bound model for CCK-B octapeptide ligands (Kolodziej et al. J. Med. Chem. 1995, 38, 137-149) and are in good agreement with the DPDPE-delta opioid receptor ''template'' model (Nikiforovich et al. Biopolymers 1991, 31, 941-955).

  DOI：

  10.1021/jm960078j

文献信息

• The Use of Topographical Constraints In Receptor Mapping:  Investigation of the Topographical Requirements of the Tryptophan 30 Residue for Receptor Binding of Asp-Tyr-<scp>d</scp>-Phe-Gly-Trp-(<i>N</i>-Me)Nle-Asp-Phe-NH₂ (SNF 9007), a Cholecystokinin (26−33) Analogue That Binds to both CCK-B and δ-Opioid Receptors
  作者：Lakmal W. Boteju、Gregory V. Nikiforovich、Carrie Haskell-Luevano、Su-Nan Fang、Teresa Zalewska、Dagmar Stropova、Henry I. Yamamura、Victor J. Hruby

  DOI：10.1021/jm960078j

  日期：1996.1.1

  The cholecystokinin (26-33) [CCK(26-33)] octapeptide analog Asp-Tyr-D-Phe-Gly-Trp(N-Me)-Nle-Asp-Phe-NH2 (SNF 9007) is a potent and selective ligand for both the CCK-B and delta-opioid receptors. Pharmacological studies of SNF 9007 suggest a relationship between the ligand requirements of CCK-B and delta-opioid receptors, which further implies a possible structural relationship between these receptors. We have utilized topographical constrainment of the important Trp(30) residue to investigate structural features of SNF 9007 that would distinguish between binding requirements in this region for the CCK-B and delta-opioid receptors, Thus, the four optically pure isomers of beta-MeTrp were substituted for L-Trp(30) Of SNF 9007. Receptor binding results suggest that the preferred topography of the Trp(30) residue for CCK-B receptor binding may be the 2S,3S (erythro-L) configuration whereas for the delta-opioid receptor it may be the 2S,3R (threo-L) configuration. Molecular modeling studies of these ligands further support the recently revised receptor-bound model for CCK-B octapeptide ligands (Kolodziej et al. J. Med. Chem. 1995, 38, 137-149) and are in good agreement with the DPDPE-delta opioid receptor ''template'' model (Nikiforovich et al. Biopolymers 1991, 31, 941-955).