(S)-2-[(S)-2-(2-{(R)-2-[(S)-2-Amino-3-(4-hydroxy-phenyl)-propionylamino]-propionylamino}-acetylamino)-3-phenyl-propionylamino]-4-methylsulfanyl-butyramide | 61090-95-7

• 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-(2-{(R)-2-[(S)-2-Amino-3-(4-hydroxy-phenyl)-propionylamino]-propionylamino}-acetylamino)-3-phenyl-propionylamino]-4-methylsulfanyl-butyramide
• 英文别名: H-Tyr-D-Ala-Gly-Phe-Met-NH2；(2S)-2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]propanoyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-4-methylsulfanylbutanamide
• CAS: 61090-95-7
• 化学式: C₂₈H₃₈N₆O₆S
• 分子量: 586.712
• InChiKey: ANZXICRKKYOVMY-SZOBAZRNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.1
• 重原子数：
  41
• 可旋转键数：
  16
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.392
• 拓扑面积：
  231
• 氢给体数：
  7
• 氢受体数：
  8

制备方法与用途

[D-Ala₂]-Met-脑啡肽是一种阿片肽，也是一种有效的阿片激动剂。它通过中枢神经系统减少胆汁流量，并且具备显著的镇痛效果[1][2]。

反应信息

• 作为反应物：
  描述：

  (S)-2-[(S)-2-(2-{(R)-2-[(S)-2-Amino-3-(4-hydroxy-phenyl)-propionylamino]-propionylamino}-acetylamino)-3-phenyl-propionylamino]-4-methylsulfanyl-butyramide 在 carboxypeptidase W 作用下， 以 水 为溶剂， 生成 蛋氨酰胺 、 L-蛋氨酸 、 L-苯丙氨酸
  参考文献：
  名称：

  Action of carboxypeptidase W on oligopeptides containing carboxy-terminally amidated peptides

  摘要：

  Carboxypeptidase W sequentially liberated amino acids from the carboxy-terminus of angiotensin I, bradykinin, delta sleep-inducing peptide and neurotensin, indicating that the sequential hydrolysis of peptides was limited by the occurrence of intermediates with the structure -Gly-X (X = L-amino acid), -Pro-X, -X-Gly and -X-Pro. The enzyme had carboxyamidase and/or amidase activities for the carboxy-terminally amidated peptides and then carboxypeptidase activity. Carboxyamidase activity of the enzyme for the carboxy-terminally amidated peptides tested was much lower than carboxypeptidase activity for Z-Glu-Tyr (Z = benzyloxycarbonyl). The enzyme essentially acted as a carboxyamidase for the long carboxy-terminally amidated peptides; an amidase became dominant for the substrates in the presence of a hydrophobic amino acid in the penultimate (P-1) or P-1 positions, especially the P-1 position, corresponding with the S-1 and S-2 sites of the enzyme. (C) 1997 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0031-9422(97)00074-5
• 作为产物：
  描述：

  N-(tert-butyloxycarbonyl)-L-tyrosyl-D-alanine 在 盐酸 、 sodium hydroxide 、 氨 、 水 、 1-羟基苯并三唑 、 溶剂黄146 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 甲醇 、 formamide 、 N,N-二甲基甲酰胺 为溶剂， 反应 1.5h， 生成 (S)-2-[(S)-2-(2-{(R)-2-[(S)-2-Amino-3-(4-hydroxy-phenyl)-propionylamino]-propionylamino}-acetylamino)-3-phenyl-propionylamino]-4-methylsulfanyl-butyramide
  参考文献：
  名称：

  Audigier; Mazarguil; Gout, European Journal of Medicinal Chemistry, 1980, vol. 15, # 2, p. 173 - 177

  摘要：

  DOI：

文献信息

• Bello, Carlo Di; Lucchiari, Adriana; Buso, Orfeo, Gazzetta Chimica Italiana, 1980, vol. 110, # 11/12, p. 617 - 620
  作者：Bello, Carlo Di、Lucchiari, Adriana、Buso, Orfeo

  DOI：——

  日期：——
• JUDD, AMRIT K.;LAWSON, JOHN A.;OLSEN, CRIS M.;TOLL, LAWRENCE R.;POLGAR, W+, INT. J. PEPTIDE AND PROTEIN RES., 30,(1987) N 3, 299-317
  作者：JUDD, AMRIT K.、LAWSON, JOHN A.、OLSEN, CRIS M.、TOLL, LAWRENCE R.、POLGAR, W+

  DOI：——

  日期：——
• Audigier; Mazarguil; Gout, European Journal of Medicinal Chemistry, 1980, vol. 15, # 2, p. 173 - 177
  作者：Audigier、Mazarguil、Gout、Cros

  DOI：——

  日期：——
• Action of carboxypeptidase W on oligopeptides containing carboxy-terminally amidated peptides
  作者：Hironori Umetsu、Kiyoshi Hishinuma、Hitoshi Wake、Michio Takeuchi、Eiji Ichishima

  DOI：10.1016/s0031-9422(97)00074-5

  日期：1997.7

  Carboxypeptidase W sequentially liberated amino acids from the carboxy-terminus of angiotensin I, bradykinin, delta sleep-inducing peptide and neurotensin, indicating that the sequential hydrolysis of peptides was limited by the occurrence of intermediates with the structure -Gly-X (X = L-amino acid), -Pro-X, -X-Gly and -X-Pro. The enzyme had carboxyamidase and/or amidase activities for the carboxy-terminally amidated peptides and then carboxypeptidase activity. Carboxyamidase activity of the enzyme for the carboxy-terminally amidated peptides tested was much lower than carboxypeptidase activity for Z-Glu-Tyr (Z = benzyloxycarbonyl). The enzyme essentially acted as a carboxyamidase for the long carboxy-terminally amidated peptides; an amidase became dominant for the substrates in the presence of a hydrophobic amino acid in the penultimate (P-1) or P-1 positions, especially the P-1 position, corresponding with the S-1 and S-2 sites of the enzyme. (C) 1997 Elsevier Science Ltd. All rights reserved.