| 726181-75-5

• 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
• CAS: 726181-75-5
• 化学式: C₅₈H₇₁N₁₇O₂₃S
• 分子量: 1406.37
• InChiKey: JNPGSPMOUUETEE-FKRLEHQTSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -6.18
• 重原子数：
  99.0
• 可旋转键数：
  36.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.34
• 拓扑面积：
  634.69
• 氢给体数：
  23.0
• 氢受体数：
  23.0

反应信息

• 作为反应物：
  描述：

  在 2,2'-二硫二吡啶 、 碳酸氢铵 作用下， 以 甲醇 为溶剂， 反应 0.5h， 以50%的产率得到
  参考文献：
  名称：

  Selective Catalysis with Peptide Dendrimers

  摘要：

  Peptide dendrimers incorporating 3,5-diaminobenzoic acid 1 as a branching unit (13) were prepared by solid-phase synthesis of ((Ac-A(3))(2)B-A(2))(2)B-Cys-A(1)-NH2 followed by disulfide bridge formation. Twenty-one homo- and heterodimeric dendrimers were obtained by permutations of aspartate, histidine, and serine at positions A(1), A(2), and A(3). Two dendrimers catalyzed the hydrolysis of 7-hydroxy-N-methyl-quinolinium esters (2-5), and two other dendrimers; catalyzed the hydrolysis of 8-hydroxy-pyrene-1,3,6-trisulfonate esters (10-12). Enzyme-like kinetics was observed in aqueous buffer pH 6.0 with multiple turnover, substrate binding (K-M = 0.1-0.5 mM), rate acceleration (k(cat)/k(uncat) > 103), and chiral discrimination (E = 2.8 for 2-phenylpropionate ester 5). The role of individual amino acids in catalysis was investigated by amino acid exchanges, highlighting the key role of histidine as a catalytic residue, and the importance of electrostatic and hydrophobic interactions in modulating substrate binding. These experiments demonstrate for the first time selective catalysis in peptide dendrimers.

  DOI：

  10.1021/ja049276n
• 作为产物：
  描述：

  乙酸酐 、 Fmoc-S-三苯甲基-L-半胱氨酸 、 (Fmoc-Asp)2O 、 二-FMOC-3,5-二氨基苯甲酸 、 (Fmoc-Ser)2O 、 alkaline earth salt of/the/ methylsulfuric acid 生成
  参考文献：
  名称：

  Selective Catalysis with Peptide Dendrimers

  摘要：

  Peptide dendrimers incorporating 3,5-diaminobenzoic acid 1 as a branching unit (13) were prepared by solid-phase synthesis of ((Ac-A(3))(2)B-A(2))(2)B-Cys-A(1)-NH2 followed by disulfide bridge formation. Twenty-one homo- and heterodimeric dendrimers were obtained by permutations of aspartate, histidine, and serine at positions A(1), A(2), and A(3). Two dendrimers catalyzed the hydrolysis of 7-hydroxy-N-methyl-quinolinium esters (2-5), and two other dendrimers; catalyzed the hydrolysis of 8-hydroxy-pyrene-1,3,6-trisulfonate esters (10-12). Enzyme-like kinetics was observed in aqueous buffer pH 6.0 with multiple turnover, substrate binding (K-M = 0.1-0.5 mM), rate acceleration (k(cat)/k(uncat) > 103), and chiral discrimination (E = 2.8 for 2-phenylpropionate ester 5). The role of individual amino acids in catalysis was investigated by amino acid exchanges, highlighting the key role of histidine as a catalytic residue, and the importance of electrostatic and hydrophobic interactions in modulating substrate binding. These experiments demonstrate for the first time selective catalysis in peptide dendrimers.

  DOI：

  10.1021/ja049276n