ethanethiol-N-tert-butyloxycarbonyl glycinamide | 162575-91-9

• 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: ethanethiol-N-tert-butyloxycarbonyl glycinamide
• 英文别名: N-Boc-glycyl-cystamine；2-(tert-butoxycarbonylaminomethylcarbonylamino)-ethyl-thiol；[(2-Mercapto-Ethylcarbamoyl)-Methyl]Carbamic Acid Tert-Butyl Ester；tert-butyl N-[2-oxo-2-(2-sulfanylethylamino)ethyl]carbamate
• CAS: 162575-91-9
• 化学式: C₉H₁₈N₂O₃S
• 分子量: 234.32
• InChiKey: AAVXNNADMXWQGS-UHFFFAOYSA-N

物化性质

• 沸点：
  426.8±30.0 °C(predicted)
• 密度：
  1.118±0.06 g/cm3(Temp: 20 °C; Press: 760 Torr)(predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.6
• 重原子数：
  15
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.78
• 拓扑面积：
  68.4
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  ethanethiol-N-tert-butyloxycarbonyl glycinamide 在 三乙基硅烷 、 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 1.5h， 生成 甘氨酰-半胱胺
  参考文献：
  名称：

  Synthesis and Evaluation of New Substrate Analogues of Streptomyces R61 dd-Peptidase:  Dissection of a Specific Ligand

  摘要：

  Good substrates of the Streptomyces R61 DD-peptidase, such as glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine, 1 (Anderson, J. W.; Pratt, R. F. Biochemistry 2000,39,12200-12209), contain the glycyl-L-alpha-amino-E-pimelyl side chain. A number of thia variants of this structure have been synthesized by means of a disconnection strategy whereby the appropriate thiols were reacted with either acryloyl-D-alanyl-D-alanine or haloalkanoyl-D-alanyl-D-alanines. Kinetics studies of the hydrolysis of these compounds by the R61 DD-peptidase showed that the presence of the N-terminal glycylammonium ion and the pimelyl-alpha-carboxylate are very important for efficient catalysis. The results of deletion of the C-terminal D-alanine indicate a promising direction toward new inhibitors. Shorter (one methylene less) and longer (one methylene more) analogues of 1 are also poor substrates. Molecular modeling and dynamics studies suggest that the higher mobility of the active site residues and the modified substrates in enzyme-substrate complexes may be the dominant factor in this loss of reactivity. The general conclusion is that essentially all of the structural elements of the side chain of 1 are required to produce a good substrate. This result has important implications for the design of inhibitors of DD-peptidases.

  DOI：

  10.1021/jo048885a
• 作为产物：
  描述：

  bis-[2-(tert-butoxycarbonylaminomethylcarbonylamino)-ethane] disulfide 在 盐酸 、 sodium tetrahydroborate 作用下， 以 甲醇 为溶剂， 生成 ethanethiol-N-tert-butyloxycarbonyl glycinamide
  参考文献：
  名称：

  Prodrug derivatives of enzyme inhibitors having hydroxyl groups, a

  摘要：

  该发明涉及酶抑制剂的前药，其中酶抑制剂中至少一个OH-基团已转化为式III、IV或V的衍生基团：##STR1## 其中R.sup.11至R.sup.25和s、l、m、o、q和r等基团如描述中所定义。这类前药在水中具有改善的溶解度和改善的药代动力学特性。

  公开号：

  US05804559A1

文献信息

• Method for analysis of reaction products
  申请人：——

  公开号：US20020090728A1

  公开（公告）日：2002-07-11

  The present invention provides methods, compounds, and kits useful in the analysis of reaction products and components of reaction mixtures, and in certain embodiments for the rapid and simultaneous determination of enantiomeric ratios, percent conversions, and absolute configurations.

  本发明提供了用于分析反应产物和反应混合物组分的方法、化合物和试剂盒，并在某些实施例中用于快速和同时确定对映体比、百分比转化率和绝对构型。
• Vesicles and other supramolecular systems made from double-tailed synthetic glycolipids derived from galactosylated tris(hydroxymethyl)aminomethane
  作者：Ange Polidori、Bernard Pucci、Leila Zarif、Jean-Michel Lacombe、Jean G. Riess、AndréA. Pavia

  DOI：10.1016/0009-3084(95)02475-x

  日期：1995.8

  A series of double-tailed hydrocarbon glycolipids derived from tris(hydroxymethyl)aminomethane (Tris) have been prepared. These amphiphiles consist of three parts: a hydrophilic head derived from mono- or polygalactosylated Tris, a linking arm of peptidic nature and a hydrophobic double tail composed of 12 or 18 carbon atom chains. The ability of the new glycolipids to disperse in water, the morphology of the self-assemblies they form and the stability of the latter were shown to depend largely on the volumetric ratio between hydrophilic head and hydrophobic tails. Comparative studies of such substrates allowed a better understanding of the relative role of the various parameters that govern the formation of tubular systems relative to vesicular organizations. In all cases, the introduction of oligomeric galactosylated heads favoured stable vesicular systems over tubules.
• US5804559A
  申请人：——

  公开号：US5804559A

  公开（公告）日：1998-09-08
• US7045360B2
  申请人：——

  公开号：US7045360B2

  公开（公告）日：2006-05-16
• Synthesis and Evaluation of New Substrate Analogues of <i>Streptomyces</i> R61 <scp>dd</scp>-Peptidase:  Dissection of a Specific Ligand
  作者：Rajesh Nagarajan、R. F. Pratt

  DOI：10.1021/jo048885a

  日期：2004.10.1

  Good substrates of the Streptomyces R61 DD-peptidase, such as glycyl-L-alpha-amino-epsilon-pimelyl-D-alanyl-D-alanine, 1 (Anderson, J. W.; Pratt, R. F. Biochemistry 2000,39,12200-12209), contain the glycyl-L-alpha-amino-E-pimelyl side chain. A number of thia variants of this structure have been synthesized by means of a disconnection strategy whereby the appropriate thiols were reacted with either acryloyl-D-alanyl-D-alanine or haloalkanoyl-D-alanyl-D-alanines. Kinetics studies of the hydrolysis of these compounds by the R61 DD-peptidase showed that the presence of the N-terminal glycylammonium ion and the pimelyl-alpha-carboxylate are very important for efficient catalysis. The results of deletion of the C-terminal D-alanine indicate a promising direction toward new inhibitors. Shorter (one methylene less) and longer (one methylene more) analogues of 1 are also poor substrates. Molecular modeling and dynamics studies suggest that the higher mobility of the active site residues and the modified substrates in enzyme-substrate complexes may be the dominant factor in this loss of reactivity. The general conclusion is that essentially all of the structural elements of the side chain of 1 are required to produce a good substrate. This result has important implications for the design of inhibitors of DD-peptidases.