(2S,3S)-2-amino-1-cyclohexyl-3-hydroxy-5-(isopropylsulfonyl)pentane | 109864-89-3

• 分子结构分类: 有机化合物 - 有机硫化合物 - 磺酰类
• 英文名称: (2S,3S)-2-amino-1-cyclohexyl-3-hydroxy-5-(isopropylsulfonyl)pentane
• 英文别名: (2S,3S)-2-amino-1-cyclohexyl-5-propan-2-ylsulfonylpentan-3-ol
• CAS: 109864-89-3
• 化学式: C₁₄H₂₉NO₃S
• 分子量: 291.455
• InChiKey: NYXYKVKRHJQXRN-KBPBESRZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  19
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  88.8
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (2S,3S)-2-amino-1-cyclohexyl-3-hydroxy-5-(isopropylsulfonyl)pentane 在 盐酸 、 1-羟基苯并三唑 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 1,4-二氧六环 、 N,N-二甲基甲酰胺 为溶剂， 反应 26.0h， 生成 N-{(S)-1-[(S)-1-[(1S,2S)-1-Cyclohexylmethyl-2-hydroxy-4-(propane-2-sulfonyl)-butylcarbamoyl]-2-(1H-imidazol-4-yl)-ethylcarbamoyl]-2-phenyl-ethyl}-3,3-dimethyl-butyramide
  参考文献：
  名称：

  Renin inhibitors. Dipeptide analogs of angiotensinogen incorporating transition-state, nonpeptidic replacements at the scissile bond

  摘要：

  A series of dipeptide analogues of angiotensinogen have been prepared and evaluated for their ability to inhibit the aspartic proteinase renin. The compounds were derived from the renin substrate by replacing the scissile amide bond with a transition-state mimic and by incorporating bioisosteric replacements for the Val-10 amide bond. Analogue 21a exhibited an IC50 of 7.6 nM against purified human renin, showed high specificity for this enzyme, and produced a hypotensive response in anesthetized, salt-depleted cynomolgus monkeys.

  DOI：

  10.1021/jm00393a008
• 作为产物：
  描述：

  (alphaS)-alpha-[[(1,1-二甲基乙氧基)羰基]氨基]-环己烷丙酸甲酯 在 barium dihydroxide 、 sodium hydroxide 、 9-borabicyclo[3.3.1]nonane dimer 、 双氧水 、 sodium hydride 、 三乙胺 、 间氯过氧苯甲酸 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 二氯甲烷 、 水 、 N,N-二甲基甲酰胺 为溶剂， 反应 43.0h， 生成 (2S,3S)-2-amino-1-cyclohexyl-3-hydroxy-5-(isopropylsulfonyl)pentane
  参考文献：
  名称：

  Renin inhibitors. Dipeptide analogs of angiotensinogen incorporating transition-state, nonpeptidic replacements at the scissile bond

  摘要：

  A series of dipeptide analogues of angiotensinogen have been prepared and evaluated for their ability to inhibit the aspartic proteinase renin. The compounds were derived from the renin substrate by replacing the scissile amide bond with a transition-state mimic and by incorporating bioisosteric replacements for the Val-10 amide bond. Analogue 21a exhibited an IC50 of 7.6 nM against purified human renin, showed high specificity for this enzyme, and produced a hypotensive response in anesthetized, salt-depleted cynomolgus monkeys.

  DOI：

  10.1021/jm00393a008

文献信息

• BOLIS, GIORGIO;FUNG, ANTHONY K. L.;GREER, JONATHAN;KLEINERT, HOLLIS D.;MA+, J. MED. CHEM., 30,(1987) N 10, 1729-1737
  作者：BOLIS, GIORGIO、FUNG, ANTHONY K. L.、GREER, JONATHAN、KLEINERT, HOLLIS D.、MA+

  DOI：——

  日期：——
• Long Acting Biologically Active Conjugates
  申请人：Silva Abelardo

  公开号：US20070207952A1

  公开（公告）日：2007-09-06

  The invention provides biologically active compounds that may be reacted with macromolecules, such as albumin, to form covalent linked complexes wherein the resulting complexes exhibit a desired biological activity in vivo. More specifically, the complexes are isolated complexes comprising a biologically active moiety covalently bound to a linking group and a protein. The complexes are prepared by conjugating a biologically active moiety, for example, a renin inhibitor or a viral fusion inhibitor peptide, with purified and isolated protein. The complexes have extended lifetimes in the bloodstream as compared to the unconjugated molecule, and exhibit biological activity for extended periods of time as compared to the unconjugated molecule. The invention also provides anti-viral compounds that are inhibitors of viral infection and/or exhibit anti-fusiogenic properties. In particular, this invention provides compounds having inhibiting activity against viruses such as human immunodeficiency virus (HIV), respiratory syncytial virus (RSV), human parainfluenza virus (HPV), measles virus (MeV), and simian immunodeficiency virus (SIV) and that have extended duration of action for the treatment of viral infections.
• Renin inhibitors. Dipeptide analogs of angiotensinogen incorporating transition-state, nonpeptidic replacements at the scissile bond
  作者：Giorgio Bolis、Anthony K. L. Fung、Jonathan Greer、Hollis D. Kleinert、Patrick A. Marcotte、Thomas J. Perun、Jacob J. Plattner、Herman H. Stein

  DOI：10.1021/jm00393a008

  日期：1987.10

  A series of dipeptide analogues of angiotensinogen have been prepared and evaluated for their ability to inhibit the aspartic proteinase renin. The compounds were derived from the renin substrate by replacing the scissile amide bond with a transition-state mimic and by incorporating bioisosteric replacements for the Val-10 amide bond. Analogue 21a exhibited an IC50 of 7.6 nM against purified human renin, showed high specificity for this enzyme, and produced a hypotensive response in anesthetized, salt-depleted cynomolgus monkeys.