((S)-1-Isopropylcarbamoyl-3-methylsulfanyl-propyl)-carbamic acid tert-butyl ester | 185065-92-3

• 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
• 英文名称: ((S)-1-Isopropylcarbamoyl-3-methylsulfanyl-propyl)-carbamic acid tert-butyl ester
• 英文别名: tert-butyl N-[(2S)-4-methylsulfanyl-1-oxo-1-(propan-2-ylamino)butan-2-yl]carbamate
• CAS: 185065-92-3
• 化学式: C₁₃H₂₆N₂O₃S
• 分子量: 290.427
• InChiKey: VTHTZSLEQGKCHE-JTQLQIEISA-N

物化性质

• 沸点：
  468.1±40.0 °C(Predicted)
• 密度：
  1.051±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  19
• 可旋转键数：
  8
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.85
• 拓扑面积：
  92.7
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  ((S)-1-Isopropylcarbamoyl-3-methylsulfanyl-propyl)-carbamic acid tert-butyl ester 在 盐酸 、 三乙胺 作用下， 以 四氢呋喃 、 1,4-二氧六环 为溶剂， 反应 1.0h， 生成 (2S)-2-(2-methylpropanoylamino)-4-methylsulfanyl-N-propan-2-ylbutanamide
  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 、 异丙胺 在 N-羟基丁二酰亚胺 、 N,N'-二环己基碳二亚胺 作用下， 生成 ((S)-1-Isopropylcarbamoyl-3-methylsulfanyl-propyl)-carbamic acid tert-butyl ester
  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

文献信息

• Redox-Triggered Secondary Structure Changes in the Aggregated States of a Designed Methionine-Rich Peptide
  作者：Heather L. Schenck、Gregory P. Dado、Samuel H. Gellman

  DOI：10.1021/ja962026p

  日期：1996.1.1

  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'').