rac-α-(4-methoxybenzylthio)-N-(tert-butoxycarbonyl)glycine | 892553-19-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: rac-α-(4-methoxybenzylthio)-N-(tert-butoxycarbonyl)glycine
• CAS: 892553-19-4
• 化学式: C₁₅H₂₁NO₅S
• 分子量: 327.401
• InChiKey: XLYUCPMBYGNNKS-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.86
• 重原子数：
  22.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.47
• 拓扑面积：
  84.86
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  rac-α-(4-methoxybenzylthio)-N-(tert-butoxycarbonyl)glycine 在 papain 、 1,4-二巯基-2,3-丁二醇 sodium hydroxide 、 disodium hydrogenphosphate 、 柠檬酸 作用下， 以 甲醇 、 正己烷 、 水 、 乙腈 、 苯 为溶剂， 反应 24.75h， 生成 (R)-tert-Butoxycarbonylamino-(4-methoxy-benzylsulfanyl)-acetic acid methyl ester
  参考文献：
  名称：

  Norcystine, a New Tool for the Study of the Structure−Activity Relationship of Peptides

  摘要：

  Norcysteine ( Ncy) is an unnatural amino acid possessing an electronegative sulfur atom directly attached to the alpha-carbon atom. We describe the synthesis of Boc-D, L-Ncy( Mob)-OH, the resolution of its methyl ester, and the introduction of both D- and L-Ncy in GnRH analogues.

  DOI：

  10.1021/ol0606740
• 作为产物：
  描述：

  氨基甲酸叔丁酯 在 对甲苯磺酸 作用下， 以 丙酮 、 苯 为溶剂， 反应 10.0h， 生成 rac-α-(4-methoxybenzylthio)-N-(tert-butoxycarbonyl)glycine
  参考文献：
  名称：

  Norcystine, a New Tool for the Study of the Structure−Activity Relationship of Peptides

  摘要：

  Norcysteine ( Ncy) is an unnatural amino acid possessing an electronegative sulfur atom directly attached to the alpha-carbon atom. We describe the synthesis of Boc-D, L-Ncy( Mob)-OH, the resolution of its methyl ester, and the introduction of both D- and L-Ncy in GnRH analogues.

  DOI：

  10.1021/ol0606740

文献信息

• Ring Size in Octreotide Amide Modulates Differently Agonist versus Antagonist Binding Affinity and Selectivity
  作者：Christy Rani R. Grace、Judit Erchegyi、Manoj Samant、Renzo Cescato、Veronique Piccand、Roland Riek、Jean Claude Reubi、Jean E. Rivier

  DOI：10.1021/jm701445q

  日期：2008.5.1

  H-DPhe(2)-c[Cys(3) -Phe(7) -DTrp(8)-Lys(9)-Thr(10)-Cys(14)] -Thr(15) -NH(2) (1) (a somatostatin agonist, SRIF numbering) and H-Cpa(2) -c[DCys(3) -Tyr(7) -DTrp(8)-Lys(9)-Thr(10)-Cys(14)] -Nal(15)-NH(2) (4) (a somatostatin antagonist) are based on the structure of octreotide that binds to three somatostatin receptor subtypes (SSt(2/3/5)) with significant binding affinity. Analogues of 1 and 4 were synthesized with norcysteine (Ncy), homocysteine (Hcy), or D-homocysteine (DHcy) at positions 3 and/or 14. Introducing Ncy at positions 3 and 14 constrained the backbone flexibility, resulting in loss of binding affinity at all sst(s) The introduction of Hey at positions 3 and 14 improved selectivity for sst(2) as a result of significant loss of binding affinity at the other ssts. Substitution by DHcy at position 3 in the antagonist scaffold (5), on the other hand, resulted in a significant loss of binding affinity at sst(2) and sst(3) as compared to the different affinities of the parent compound (4). The 3D NMR structures of the analogues in dimethylsulfoxide are consistent with the observed binding affinities.
• Ring Size of Somatostatin Analogues (ODT-8) Modulates Receptor Selectivity and Binding Affinity
  作者：Judit Erchegyi、Christy Rani R. Grace、Manoj Samant、Renzo Cescato、Veronique Piccand、Roland Riek、Jean Claude Reubi、Jean E. Rivier

  DOI：10.1021/jm701444y

  日期：2008.5.1

  The synthesis, biological testing, and NMR studies of several analogues of H-c[Cys(3) -Phe(6) -Phe(7) -DTrp(8)- Lys(9)-Thr(10)-Phe(11)-CYS(14)] -OH (ODT-8, a pan-somatostatin analogue, 1) have been performed to assess the effect of changing the stereochemistry and the number of atoms in the disulfide bridge on binding affinity. Cysteine at positions 3 and/or 14 (somatostatin numbering) were/was substituted with D-Cysteine, norcysteine, D-norcysteine, homocysteine, and/or D-homocysteine. The 3D structure analysis of selected partially selective, bioactive analogues (3, 18, 19, and 21) was carried out in dim ethyl sulfoxide. Interestingly and not unexpectedly, the 3D structures of these analogues comprised the pharmacophore for which the analogues had the highest binding affinities (i.e., sst(4) in all cases).