((S)-2-Hydroxy-1-isobutyl-hexyl)-carbamic acid benzyl ester | 207728-35-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: ((S)-2-Hydroxy-1-isobutyl-hexyl)-carbamic acid benzyl ester
• CAS: 207728-35-6
• 化学式: C₁₈H₂₉NO₃
• 分子量: 307.433
• InChiKey: FFRYEPVMJYMJLH-BHWOMJMDSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.88
• 重原子数：
  22.0
• 可旋转键数：
  9.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.61
• 拓扑面积：
  58.56
• 氢给体数：
  2.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  ((S)-2-Hydroxy-1-isobutyl-hexyl)-carbamic acid benzyl ester 在 palladium on activated charcoal 氢气 、 溶剂黄146 作用下， 以 甲醇 为溶剂， 以89%的产率得到Leuψ(CHOH)(CH₂)₃CH₃
  参考文献：
  名称：

  Auxiliary Agents for the Peroral Administration of Peptide and Protein Drugs:  Synthesis and Evaluation of Novel Pepstatin Analogues

  摘要：

  The peroral administration of(poly)peptide drugs requires the development of delivery systems, which provide a protective effect toward a gastrointestinal enzymatic attack. A promising strategy for such systems represents polymer-enzyme inhibitor conjugates in which the embedded therapeutic agent is protected. However, the practical use of polymer-inhibitor conjugates has so far been limited by high production costs of these auxiliary agents. To solve this problem for delivery systems shielding from pepsinic degradation, structurally simplified analogues of the pepsin inhibitor pepstatin A have been synthesized. The synthesis of tripeptide analogues, described by McConnell et al., led us to pursue further modifications varying the C-terminus. Our target to attach a spacer moisty-enabling the free access of pepsin to the inhibitor-should be combined with an attractive synthetic approach providing low production costs in large-scale preparation. Structure modifications comprised either the side chain of the third amino acid which served as starting compound designing the C-terminus (L-leucine, L-isoleucine, L-norvaline) as the length of the spacer link, simulated by a linear alkyl group (n-butyl, n-hexyl, and n-octyl). The inhibitory activities which have been evaluated by an enzyme assay were significantly dependent on the nature of the side chain, whereas the length of the spacer had no influence on the inhibitory effect. Analogues bearing the isobutyl or n-propyl moiety as side chain displayed a strong inhibitory effect which was comparable to that pepstatin A. These congeners represent promising auxiliary agents for the peroral administration of(poly)peptide drugs.

  DOI：

  10.1021/jm980015w
• 作为产物：
  描述：

  benzyl N-[(4S)-2-methyl-5-oxononan-4-yl]carbamate 在 sodium tetrahydroborate 作用下， 以 甲醇 为溶剂， 反应 0.5h， 以91%的产率得到((S)-2-Hydroxy-1-isobutyl-hexyl)-carbamic acid benzyl ester
  参考文献：
  名称：

  Auxiliary Agents for the Peroral Administration of Peptide and Protein Drugs:  Synthesis and Evaluation of Novel Pepstatin Analogues

  摘要：

  The peroral administration of(poly)peptide drugs requires the development of delivery systems, which provide a protective effect toward a gastrointestinal enzymatic attack. A promising strategy for such systems represents polymer-enzyme inhibitor conjugates in which the embedded therapeutic agent is protected. However, the practical use of polymer-inhibitor conjugates has so far been limited by high production costs of these auxiliary agents. To solve this problem for delivery systems shielding from pepsinic degradation, structurally simplified analogues of the pepsin inhibitor pepstatin A have been synthesized. The synthesis of tripeptide analogues, described by McConnell et al., led us to pursue further modifications varying the C-terminus. Our target to attach a spacer moisty-enabling the free access of pepsin to the inhibitor-should be combined with an attractive synthetic approach providing low production costs in large-scale preparation. Structure modifications comprised either the side chain of the third amino acid which served as starting compound designing the C-terminus (L-leucine, L-isoleucine, L-norvaline) as the length of the spacer link, simulated by a linear alkyl group (n-butyl, n-hexyl, and n-octyl). The inhibitory activities which have been evaluated by an enzyme assay were significantly dependent on the nature of the side chain, whereas the length of the spacer had no influence on the inhibitory effect. Analogues bearing the isobutyl or n-propyl moiety as side chain displayed a strong inhibitory effect which was comparable to that pepstatin A. These congeners represent promising auxiliary agents for the peroral administration of(poly)peptide drugs.

  DOI：

  10.1021/jm980015w