FGGF-NH2 | 173910-41-3

• 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: FGGF-NH2
• 英文别名: L-Phenylalaninamide, L-phenylalanylglycylglycyl-；(2S)-2-amino-N-[2-[[2-[[(2S)-1-amino-1-oxo-3-phenylpropan-2-yl]amino]-2-oxoethyl]amino]-2-oxoethyl]-3-phenylpropanamide
• CAS: 173910-41-3
• 化学式: C₂₂H₂₇N₅O₄
• 分子量: 425.487
• InChiKey: VQMNJURNUPNOLE-ROUUACIJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.1
• 重原子数：
  31
• 可旋转键数：
  11
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  156
• 氢给体数：
  5
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  Fmoc-甘氨酸 、 Fmoc-L-苯丙氨酸 、 alkaline earth salt of/the/ methylsulfuric acid 生成 FGGF-NH2
  参考文献：
  名称：

  Address and Message Sequences for the Nociceptin Receptor:  A Structure−Activity Study of Nociceptin-(1−13)-peptide amide

  摘要：

  Nociceptin (NC) and some of its fragments as well as nociceptin-(1-13)-peptide amide [NC(1-13)-NH2] and a series of its analogues were prepared and tested in the mouse vas deferens in an attempt to identify the sequences involved in the activation (message) and in the binding (address) of nociceptin to its receptor. The NC receptor that inhibits the electrically evoked twitches of the mouse vas deferens was demonstrated to be distinct from the delta opioid receptor, since naloxone and Dmt-Tic-OH (a selective delta opioid receptor antagonist) block the delta opioid receptor but have no effect on the nociceptin receptor. Results from structure-activity experiments suggest that (a) the entire sequence of NC may not be required for full biological activities, since NC(1-13)-NH2 is as active as NC; (b) fragments of NC have however to be amidated as in NC(1-13)-NH2 in order to be protected from degradation by proteases; (c) cationic residues (as Args(8,12), Lys(9,13)) appear to play a functional role, since their replacement with Ala in the sequence of NC(1-13)-NH2 leads to inactivity; (d) the N-terminal tetrapeptide Phe-Gly-Gly-Phe is essential for activity: its full length and flexibility appear to be required for NC receptor activation and/or occupation; (e) Phe(4) and not Phe(1) appears to be the residue involved in receptor activation, since the replacement of Phe(1) with Leu has no effect, while that of Phe(4) leads to inactivity. Results summarized in this paper indicate that the structural requirements of NC for occupation and activation of its receptor are different from that of opioids, particularly delta agonists.

  DOI：

  10.1021/jm970011b

文献信息

• Address and Message Sequences for the Nociceptin Receptor:  A Structure−Activity Study of Nociceptin-(1−13)-peptide amide
  作者：Remo Guerrini、Girolamo Calo'、Anna Rizzi、Clementina Bianchi、Lawrence H. Lazarus、Severo Salvadori、Piero A. Temussi、Domenico Regoli

  DOI：10.1021/jm970011b

  日期：1997.6.1

  Nociceptin (NC) and some of its fragments as well as nociceptin-(1-13)-peptide amide [NC(1-13)-NH2] and a series of its analogues were prepared and tested in the mouse vas deferens in an attempt to identify the sequences involved in the activation (message) and in the binding (address) of nociceptin to its receptor. The NC receptor that inhibits the electrically evoked twitches of the mouse vas deferens was demonstrated to be distinct from the delta opioid receptor, since naloxone and Dmt-Tic-OH (a selective delta opioid receptor antagonist) block the delta opioid receptor but have no effect on the nociceptin receptor. Results from structure-activity experiments suggest that (a) the entire sequence of NC may not be required for full biological activities, since NC(1-13)-NH2 is as active as NC; (b) fragments of NC have however to be amidated as in NC(1-13)-NH2 in order to be protected from degradation by proteases; (c) cationic residues (as Args(8,12), Lys(9,13)) appear to play a functional role, since their replacement with Ala in the sequence of NC(1-13)-NH2 leads to inactivity; (d) the N-terminal tetrapeptide Phe-Gly-Gly-Phe is essential for activity: its full length and flexibility appear to be required for NC receptor activation and/or occupation; (e) Phe(4) and not Phe(1) appears to be the residue involved in receptor activation, since the replacement of Phe(1) with Leu has no effect, while that of Phe(4) leads to inactivity. Results summarized in this paper indicate that the structural requirements of NC for occupation and activation of its receptor are different from that of opioids, particularly delta agonists.