| 185065-94-5

• 分子结构分类: 有机化合物 - 有机硫化合物 - 亚砜
• CAS: 185065-94-5
• 化学式: C₁₂H₂₄N₂O₃S
• 分子量: 276.4
• InChiKey: ZYEFLZANOJPHFQ-APDXDRDNSA-N

物化性质

• 沸点：
  587.3±45.0 °C(Predicted)
• 密度：
  1.109±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  0.42
• 重原子数：
  18.0
• 可旋转键数：
  7.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.83
• 拓扑面积：
  75.27
• 氢给体数：
  2.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  在 甲酸 、 双氧水 作用下， 以 二氯甲烷 为溶剂， 反应 18.0h， 以100%的产率得到
  参考文献：
  名称：

  Redox-Triggered Secondary Structure Changes in the Aggregated States of a Designed Methionine-Rich Peptide

  摘要：

  We have previously shown that methionine can be used as a ''switchable'' residue for the design of peptides with alternative secondary structure preferences in the aggregated state (J. Am. Chem. Sec. 1993, 115, 12609). Redox-induced secondary structure changes in the 18-residue peptide Ac-YLKAMLEAMAKLMAKLMA-NH2 result from conversion of lipophilic methionine (M) to hydrophilic methionine sulfoxide (M degrees), which transforms a peptide capable of adopting an amphiphilic alpha-helical conformation into a peptide capable of adopting an amphiphilic beta-strand conformation. Here we present a detailed characterization of the third oxidation state of this peptide, in which the methionine residues are oxidized to the sulfone state. The sulfone form behaves similarly to the sulfoxide form, even though the sulfone group is somewhat less hydrophilic than the sulfoxide group. These results provide support for the concept that the conformational preferences of peptides and proteins are strongly dependent upon the linear ordering of hydrophilic and lipophilic residues (''amphiphilic order'').

  DOI：

  10.1021/ja962026p
• 作为产物：
  描述：

  Boc-L-蛋氨酸 在 盐酸 、 N-羟基丁二酰亚胺 、 双氧水 、 溶剂黄146 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 四氢呋喃 、 1,4-二氧六环 、 二氯甲烷 为溶剂， 反应 24.0h， 生成
  参考文献：
  名称：

  Redox-Triggered Secondary Structure Changes in the Aggregated States of a Designed Methionine-Rich Peptide

  摘要：

  We have previously shown that methionine can be used as a ''switchable'' residue for the design of peptides with alternative secondary structure preferences in the aggregated state (J. Am. Chem. Sec. 1993, 115, 12609). Redox-induced secondary structure changes in the 18-residue peptide Ac-YLKAMLEAMAKLMAKLMA-NH2 result from conversion of lipophilic methionine (M) to hydrophilic methionine sulfoxide (M degrees), which transforms a peptide capable of adopting an amphiphilic alpha-helical conformation into a peptide capable of adopting an amphiphilic beta-strand conformation. Here we present a detailed characterization of the third oxidation state of this peptide, in which the methionine residues are oxidized to the sulfone state. The sulfone form behaves similarly to the sulfoxide form, even though the sulfone group is somewhat less hydrophilic than the sulfoxide group. These results provide support for the concept that the conformational preferences of peptides and proteins are strongly dependent upon the linear ordering of hydrophilic and lipophilic residues (''amphiphilic order'').

  DOI：

  10.1021/ja962026p