6-cyano-6-methyl-9-oxo-4-thioxo-10,13-dioxa-3,5-dithiapentadecan-15-yl 6-oxo-6-(2-thioxothiazolidin-3-yl)hexanoate | 1217549-61-5

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: 6-cyano-6-methyl-9-oxo-4-thioxo-10,13-dioxa-3,5-dithiapentadecan-15-yl 6-oxo-6-(2-thioxothiazolidin-3-yl)hexanoate
• 英文别名: 2-[2-[6-Oxo-6-(2-sulfanylidene-1,3-thiazolidin-3-yl)hexanoyl]oxyethoxy]ethyl 4-cyano-4-ethylsulfanylcarbothioylsulfanylpentanoate；2-[2-[6-oxo-6-(2-sulfanylidene-1,3-thiazolidin-3-yl)hexanoyl]oxyethoxy]ethyl 4-cyano-4-ethylsulfanylcarbothioylsulfanylpentanoate
• CAS: 1217549-61-5
• 化学式: C₂₂H₃₂N₂O₆S₅
• 分子量: 580.836
• InChiKey: BYTJBZJHXJEYTI-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  35
• 可旋转键数：
  20
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.73
• 拓扑面积：
  246
• 氢给体数：
  0
• 氢受体数：
  12

反应信息

• 作为产物：
  描述：

  4-氰基-4-(((乙硫基)硫代羰基)硫基)戊酸 在 2-(dimethylamino)pyridinium p-toluenesulfonate 、 N,N'-二环己基碳二亚胺 作用下， 以 二氯甲烷 为溶剂， 反应 10.0h， 生成 6-cyano-6-methyl-9-oxo-4-thioxo-10,13-dioxa-3,5-dithiapentadecan-15-yl 6-oxo-6-(2-thioxothiazolidin-3-yl)hexanoate
  参考文献：
  名称：

  Synthesis, Characterization, and Bioactivity of Mid-Functional PolyHPMA−Lysozyme Bioconjugates

  摘要：

  A thiazolidine-2-thione mid-functionalized chain transfer agent (CTA) was synthesized and used as a reversible addition fragmentation chain transfer (RAFT) polymerization agent to prepare poly(N-(2-hydroxypropyl)methacrylamide) (polyHPMA) with mid-chain thiazolidine-2-thione functionality. The synthesized polymers were fully analyzed by H-1 NMR and GPC, confirming well-defined structures (predesigned molecular weights, narrow polydispersities, and high functionalization efficiencies). A subsequent hydrolysis/analysis of the polymers was performed to verify their mid-functional structures. These mid-functionalized polymers were then incubated with a model protein (lysozyme) to generate branched polymer protein bioconjugates. The bioactivity of the branched polymer protein conjugate was tested and compared to similar molecular weight linear polyHPMA-protein bioconjugate; the branched polymer protein conjugate remained much more protein activity, indicating the mid-chain-functional polyHPMA was more selective in its conjugation reaction on the lysozyme surface when compared with conjugation reactions involving terminal-functional polyHPMA. This straightforward methodology, described herein, for the synthesis of branched polymer protein bioconjugates strikes a balance between protein protection by the attachment of polymer chains and the subsequent bioactivity retention of the bioconjugate.

  DOI：

  10.1021/ma100142w

文献信息

• Synthesis, Characterization, and Bioactivity of Mid-Functional PolyHPMA−Lysozyme Bioconjugates
  作者：Lei Tao、Jiangtao Xu、David Gell、Thomas P. Davis

  DOI：10.1021/ma100142w

  日期：2010.4.27

  A thiazolidine-2-thione mid-functionalized chain transfer agent (CTA) was synthesized and used as a reversible addition fragmentation chain transfer (RAFT) polymerization agent to prepare poly(N-(2-hydroxypropyl)methacrylamide) (polyHPMA) with mid-chain thiazolidine-2-thione functionality. The synthesized polymers were fully analyzed by H-1 NMR and GPC, confirming well-defined structures (predesigned molecular weights, narrow polydispersities, and high functionalization efficiencies). A subsequent hydrolysis/analysis of the polymers was performed to verify their mid-functional structures. These mid-functionalized polymers were then incubated with a model protein (lysozyme) to generate branched polymer protein bioconjugates. The bioactivity of the branched polymer protein conjugate was tested and compared to similar molecular weight linear polyHPMA-protein bioconjugate; the branched polymer protein conjugate remained much more protein activity, indicating the mid-chain-functional polyHPMA was more selective in its conjugation reaction on the lysozyme surface when compared with conjugation reactions involving terminal-functional polyHPMA. This straightforward methodology, described herein, for the synthesis of branched polymer protein bioconjugates strikes a balance between protein protection by the attachment of polymer chains and the subsequent bioactivity retention of the bioconjugate.