Lys(N^ε-Boc)-Gly-NH2 | 56675-35-5

• 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: Lys(N^ε-Boc)-Gly-NH2
• 英文别名: tert-butyl N-[(5S)-5-amino-6-[(2-amino-2-oxoethyl)amino]-6-oxohexyl]carbamate
• CAS: 56675-35-5
• 化学式: C₁₃H₂₆N₄O₄
• 分子量: 302.374
• InChiKey: BYKXFOWGKVVVCN-VIFPVBQESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.6
• 重原子数：
  21
• 可旋转键数：
  10
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.77
• 拓扑面积：
  137
• 氢给体数：
  4
• 氢受体数：
  5

反应信息

• 作为产物：
  描述：

  Nε-Boc-Nα-Cbz-L-赖氨酸 在 palladium on activated charcoal 氢气 、 N,N'-二环己基碳二亚胺 作用下， 生成 Lys(N^ε-Boc)-Gly-NH2
  参考文献：
  名称：

  Synthèse de l'Ala¹-Ala⁶-Arg⁸-vasopressine et de l'Ala¹-Ala⁶-Lys⁸-vasopressine, ainsi que de la (déamino-Ala)¹-Ala⁶-Arg⁸-vasopressine et de la (désamino-Ala)¹-Ala⁶-Lys⁸-vasopressine

  摘要：

  AbstractAla1‐Ala6‐Arg8‐vasopressin, Ala1‐Ala6‐Lys8‐vasopressin, (Deamino‐Ala)1‐Ala6‐Arg8‐vasopressin and (Deamino‐Ala)1‐Ala6‐Lys8‐vasopressin were prepared by condensation of a tripeptide azide or, respectively, a propionyl‐dipeptide azide with a hexapeptide amide, both fragments having been synthesized by methods excluding racemization. These peptides represent analogues of arginine‐vasopressin, lysinevasopressin and of their deamino derivatives, in which the ring is open and the sulphur atoms are replaced by hydrogen atoms. The new peptides were found to be devoid of any biological activity and did not inhibit the corresponding natural hormones. The significance of this observation is discussed.

  DOI：

  10.1002/hlca.19650480807

文献信息

• Synthèse de l'Ala¹-Ala⁶-Arg⁸-vasopressine et de l'Ala¹-Ala⁶-Lys⁸-vasopressine, ainsi que de la (déamino-Ala)¹-Ala⁶-Arg⁸-vasopressine et de la (désamino-Ala)¹-Ala⁶-Lys⁸-vasopressine
  作者：R. L. Huguenin、St. Guttmann

  DOI：10.1002/hlca.19650480807

  日期：——

  AbstractAla1‐Ala6‐Arg8‐vasopressin, Ala1‐Ala6‐Lys8‐vasopressin, (Deamino‐Ala)1‐Ala6‐Arg8‐vasopressin and (Deamino‐Ala)1‐Ala6‐Lys8‐vasopressin were prepared by condensation of a tripeptide azide or, respectively, a propionyl‐dipeptide azide with a hexapeptide amide, both fragments having been synthesized by methods excluding racemization. These peptides represent analogues of arginine‐vasopressin, lysinevasopressin and of their deamino derivatives, in which the ring is open and the sulphur atoms are replaced by hydrogen atoms. The new peptides were found to be devoid of any biological activity and did not inhibit the corresponding natural hormones. The significance of this observation is discussed.