(3R,6S,8aS)-6-Benzyloxycarbonylamino-5-oxo-hexahydro-thiazolo[3,2-a]pyridine-3-carboxylic acid | 160248-47-5

• 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: (3R,6S,8aS)-6-Benzyloxycarbonylamino-5-oxo-hexahydro-thiazolo[3,2-a]pyridine-3-carboxylic acid
• CAS: 160248-47-5
• 化学式: C₁₆H₁₈N₂O₅S
• 分子量: 350.395
• InChiKey: UVQNUWZXKSZFNI-AVGNSLFASA-N

物化性质

• 沸点：
  648.6±55.0 °C(Predicted)
• 密度：
  1.45±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  1.43
• 重原子数：
  24.0
• 可旋转键数：
  4.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  95.94
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  (3R,6S,8aS)-6-Benzyloxycarbonylamino-5-oxo-hexahydro-thiazolo[3,2-a]pyridine-3-carboxylic acid 在 氢溴酸 、 sodium carbonate 作用下， 以 乙二醇二甲醚 、 乙酸乙酯 为溶剂， 反应 3.17h， 生成 Fmoc-β-turn-dipeptide
  参考文献：
  名称：

  Cyclic Hexapeptides and Chimeric Peptides as Mimics of Tendamistat

  摘要：

  We describe the design and evaluation of structural mimics of tendamistat, a 74-residue proteinaceous inhibitor of alpha-amylase. Cyclic hexapeptides were designed in which the sequence Trp-Arg-Tyr is constrained to the i + 1 to i + 3 positions of a type I beta-turn; these compounds inhibit alpha-amylase with K-i values of 14-32 mu M, significantly more tightly than related linear tri- and hexapeptides. Incorporation of the bicyclic Nagai-Sato type II beta-turn mimic opposite the Trp-Arg-Tyr sequence in a chimeric molecule leads to a weaker inhibitor. NMR studies indicate that the desired beta-turn conformation is adopted by the cyclic hexapeptides but not by the chimeric molecule, supporting the interpretation that the former are indeed acting as small molecule mimics of tendamistat.

  DOI：

  10.1021/ja00102a008
• 作为产物：
  描述：

  (S)-4-<2'-(Chloroformyl)ethyl>-5-oxooxazolidin-3-carbonsaeure-benzylester 在 吡啶 、 sodium hydroxide 、 三正丁基氢锡 、 sodium carbonate 作用下， 以 甲醇 、 乙酸乙酯 为溶剂， 反应 142.0h， 生成 (3R,6S,8aS)-6-Benzyloxycarbonylamino-5-oxo-hexahydro-thiazolo[3,2-a]pyridine-3-carboxylic acid
  参考文献：
  名称：

  Cyclic Hexapeptides and Chimeric Peptides as Mimics of Tendamistat

  摘要：

  We describe the design and evaluation of structural mimics of tendamistat, a 74-residue proteinaceous inhibitor of alpha-amylase. Cyclic hexapeptides were designed in which the sequence Trp-Arg-Tyr is constrained to the i + 1 to i + 3 positions of a type I beta-turn; these compounds inhibit alpha-amylase with K-i values of 14-32 mu M, significantly more tightly than related linear tri- and hexapeptides. Incorporation of the bicyclic Nagai-Sato type II beta-turn mimic opposite the Trp-Arg-Tyr sequence in a chimeric molecule leads to a weaker inhibitor. NMR studies indicate that the desired beta-turn conformation is adopted by the cyclic hexapeptides but not by the chimeric molecule, supporting the interpretation that the former are indeed acting as small molecule mimics of tendamistat.

  DOI：

  10.1021/ja00102a008

文献信息

• Conformationally constrained inhibitors of caspase-1 (interleukin-1β converting enzyme) and of the human ced-3 homologue caspase-3 (CPP32, apopain)
  作者：Donald S. Karanewsky、Xu Bai、Steven D. Linton、Joseph F. Krebs、Joe Wu、Bryan Pham、Kevin J. Tomaselli

  DOI：10.1016/s0960-894x(98)00498-3

  日期：1998.10

  A systematic study of interleukin-lp converting enzyme (ICE, caspase-1) and caspase-3 (CPP32, apopain) inhibitors incorporating a PGammaP3 conformationally constrained dipeptide mimetic is reported. Depending on the nature of the P-4 substituent, highly selective inhibitors of both Csp-l or Csp-3 were obtained. (C) 1998 Elsevier Science Ltd. All rights reserved.