1,2,3-Trimethoxy-5-[(4-methylphenyl)methylsulfanyl]benzene | 433935-38-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯酚醚
• 英文名称: 1,2,3-Trimethoxy-5-[(4-methylphenyl)methylsulfanyl]benzene
• 英文别名: 1,2,3-trimethoxy-5-[(4-methylphenyl)methylsulfanyl]benzene
• CAS: 433935-38-7
• 化学式: C₁₇H₂₀O₃S
• 分子量: 304.41
• InChiKey: CXKRMJBIVLWTHA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.2
• 重原子数：
  21
• 可旋转键数：
  6
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  53
• 氢给体数：
  0
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  1,2,3-Trimethoxy-5-[(4-methylphenyl)methylsulfanyl]benzene 在 羟胺 、 三乙胺 、 三氯氧磷 作用下， 以 二氯甲烷 为溶剂， 反应 20.0h， 生成
  参考文献：
  名称：

  Extending Synthetic Access to Proteins with a Removable Acyl Transfer Auxiliary

  摘要：

  A chemo- and regioselective auxiliary-mediated peptide ligation has been developed that is effective under nonidealized conditions for the synthesis of proteins. This general amide bond ligation utilizes a removable auxiliary that is analogous to the role of cysteine in native chemical ligation, combining chemoselective thioester exchange with efficient regioselective intramolecular acyl transfer. Acid lability and improved ligation efficiency were introduced into the 2-mercaptobenzyl auxiliary by increasing the electron density of the aromatic ring. The 62 amino acid SH3 domain from a-spectrin was synthesized using the auxiliary-mediated ligation at a Lys-Gly sequence. The auxiliary was removed with TFA and scavengers from the ligated product. This methodology enables unprotected peptides to be coupled at noncysteine ligation sites expanding the scope of protein synthesis and semisynthesis.

  DOI：

  10.1021/ja016731w
• 作为产物：
  描述：

  O-ethyl S-(3,4,5-trimethoxyphenyl)carbonodithioate 在 sodium hydroxide 、 sodium hydride 作用下， 以 四氢呋喃 、 甲醇 、 乙醇 为溶剂， 反应 2.33h， 生成 1,2,3-Trimethoxy-5-[(4-methylphenyl)methylsulfanyl]benzene
  参考文献：
  名称：

  Extending Synthetic Access to Proteins with a Removable Acyl Transfer Auxiliary

  摘要：

  A chemo- and regioselective auxiliary-mediated peptide ligation has been developed that is effective under nonidealized conditions for the synthesis of proteins. This general amide bond ligation utilizes a removable auxiliary that is analogous to the role of cysteine in native chemical ligation, combining chemoselective thioester exchange with efficient regioselective intramolecular acyl transfer. Acid lability and improved ligation efficiency were introduced into the 2-mercaptobenzyl auxiliary by increasing the electron density of the aromatic ring. The 62 amino acid SH3 domain from a-spectrin was synthesized using the auxiliary-mediated ligation at a Lys-Gly sequence. The auxiliary was removed with TFA and scavengers from the ligated product. This methodology enables unprotected peptides to be coupled at noncysteine ligation sites expanding the scope of protein synthesis and semisynthesis.

  DOI：

  10.1021/ja016731w

文献信息

• Extending Synthetic Access to Proteins with a Removable Acyl Transfer Auxiliary
  作者：John Offer、C. N. C. Boddy、Philip E. Dawson

  DOI：10.1021/ja016731w

  日期：2002.5.1

  A chemo- and regioselective auxiliary-mediated peptide ligation has been developed that is effective under nonidealized conditions for the synthesis of proteins. This general amide bond ligation utilizes a removable auxiliary that is analogous to the role of cysteine in native chemical ligation, combining chemoselective thioester exchange with efficient regioselective intramolecular acyl transfer. Acid lability and improved ligation efficiency were introduced into the 2-mercaptobenzyl auxiliary by increasing the electron density of the aromatic ring. The 62 amino acid SH3 domain from a-spectrin was synthesized using the auxiliary-mediated ligation at a Lys-Gly sequence. The auxiliary was removed with TFA and scavengers from the ligated product. This methodology enables unprotected peptides to be coupled at noncysteine ligation sites expanding the scope of protein synthesis and semisynthesis.