methyl (2S)-2-amino-4-(tritylsulfanyl)butanoate | 259822-63-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: methyl (2S)-2-amino-4-(tritylsulfanyl)butanoate
• CAS: 259822-63-4
• 化学式: C₂₄H₂₅NO₂S
• 分子量: 391.534
• InChiKey: KPMZEXRNWXMOSD-QFIPXVFZSA-N

物化性质

• 沸点：
  511.7±50.0 °C(Predicted)
• 密度：
  1.162±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  4.6
• 重原子数：
  28.0
• 可旋转键数：
  8.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.21
• 拓扑面积：
  52.32
• 氢给体数：
  1.0
• 氢受体数：
  4.0

反应信息

• 作为反应物：
  描述：

  methyl (2S)-2-amino-4-(tritylsulfanyl)butanoate 在 吡啶 、 三乙基硅烷 、 二甲基硫 、 四溴化碳 、 水 、 O-(1H-benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium hexafluorophosphate 、 1,8-二氮杂双环[5.4.0]十一碳-7-烯 、 N,N-二异丙基乙胺 、 三苯基膦 、 三氟乙酸 、 三甲基膦 作用下， 以 四氢呋喃 、 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 生成 (8S,14S)-14-{[1-Acetyl-3-(4-hydroxy-phenyl)-pyrrolidine-2-carbonyl]-amino}-6,15-dioxo-11-thia-7,16-diaza-spiro[4.13]octadecane-8-carboxylic acid methyl ester
  参考文献：
  名称：

  Cyclic thioether peptide mimetics as VCAM–VLA-4 antagonists

  摘要：

  Selective substitution of a sulfur atom by carbon in a highly potent 13-membered cyclic disulfide was accomplished by intramolecular displacement of a bromide. The potency of the resulting thioethers in the VCAM/VLA-4 assay was dependant on rin size and the position of the sulfur atom. (C) 2000 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0960-894x(00)00175-x
• 作为产物：
  描述：

  2-bromoethyl triphenylmethyl sulfide 在 1,3-二甲基-2-咪唑啉酮 、 盐酸 、 正丁基锂 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 正己烷 为溶剂， 反应 26.75h， 生成 methyl (2S)-2-amino-4-(tritylsulfanyl)butanoate
  参考文献：
  名称：

  The first asymmetric syntheses of l-homocysteine and l-homocystine

  摘要：

  Asymmetric syntheses of L-homocysteine 1 and L-homocystine 2 are described. Alkylation of the carbanion derived from Schollkopf reagent 3 and ensuing hydrolyses gave S-triphenylmethyl-L-homocysteine 6, Removal of the triphenylmethyl group gave L-homocysteine 1 and subsequent oxidation provided L-homocystine 2. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(99)00453-x

文献信息

• Mercury binding by ferrocenoyl peptides with sulfur-containing side chains: Electrochemical, spectroscopic and structural studies
  作者：Conor C.G. Scully、Paul Jensen、Peter J. Rutledge

  DOI：10.1016/j.jorganchem.2008.06.005

  日期：2008.8

  Ferrocenoyl peptides incorporating amino acids derived from either L- methionine, L- cysteine or DL- homocysteine have been synthesised and investigated as agents for heavy metal binding and detection. Heavy metal - peptide interactions have been characterised using cyclic voltammetry to follow changes in the potential of the Fe( II)/ Fe( III) redox couple, revealing that these systems interact with mercury( II) ions more strongly than with other thiophilic heavy metals such as cadmium( II), silver( I) and lead( II). Proton NMR experiments have demonstrated 1: 1 peptide: mercury binding and enabled quantitative characterisation of this binding interaction. Crystal structures for two of these ferrocenoyl peptide derivatives have been elucidated, revealing that these compounds adopt a P- 1,30 open solid state conformation in the absence of mercury; this arrangement precludes intramolecular hydrogen bonding between chains, while extensive intermolecular hydrogen bonding is evident. The particular af. nity of these systems for mercury( II) opens the possibility of incorporating them in new, biologically inspired sensors for detecting this toxic pollutant. (c) 2008 Elsevier B. V. All rights reserved.