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(R)-2-Trifluoromethanesulfonyloxy-succinic acid dimethyl ester | 171049-36-8

中文名称
——
中文别名
——
英文名称
(R)-2-Trifluoromethanesulfonyloxy-succinic acid dimethyl ester
英文别名
Dimethyl (r)-malate o-triflate;dimethyl (2R)-2-(trifluoromethylsulfonyloxy)butanedioate
(R)-2-Trifluoromethanesulfonyloxy-succinic acid dimethyl ester化学式
CAS
171049-36-8
化学式
C7H9F3O7S
mdl
——
分子量
294.205
InChiKey
VTGAHMHUTNTATF-SCSAIBSYSA-N
BEILSTEIN
——
EINECS
——
  • 物化性质
  • 计算性质
  • ADMET
  • 安全信息
  • SDS
  • 制备方法与用途
  • 上下游信息
  • 反应信息
  • 文献信息
  • 表征谱图
  • 同类化合物
  • 相关功能分类
  • 相关结构分类

计算性质

  • 辛醇/水分配系数(LogP):
    0.6
  • 重原子数:
    18
  • 可旋转键数:
    7
  • 环数:
    0.0
  • sp3杂化的碳原子比例:
    0.71
  • 拓扑面积:
    104
  • 氢给体数:
    0
  • 氢受体数:
    10

反应信息

  • 作为反应物:
    描述:
    ((1S,3S)-3-Amino-2,2-dimethyl-cyclopropyl)-methanol 、 (R)-2-Trifluoromethanesulfonyloxy-succinic acid dimethyl ester2,6-二甲基吡啶N,N-二异丙基乙胺 作用下, 以 二氯甲烷 为溶剂, 生成 (S)-2-((1S,3S)-3-Hydroxymethyl-2,2-dimethyl-cyclopropylamino)-succinic acid dimethyl ester
    参考文献:
    名称:
    Design and synthesis of conformationally constrained, extended and reverse turn pseudopeptides as Grb2-SH2 domain antagonists
    摘要:
    A series of conformationally constrained and flexible pseudopeptide derivatives of the tripeptide pYVN were prepared as potential antagonists of interactions of phosphotyrosine peptides with the Grb2-SH2 domain. The conformation ally constrained compounds contained trans- and cis-cyclopropanes as replacements to enforce locally extended and reverse turn peptide conformations, respectively. (C) 2003 Elsevier Science Ltd. All rights reserved.
    DOI:
    10.1016/s0040-4039(03)00013-3
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文献信息

  • Design and synthesis of conformationally constrained, extended and reverse turn pseudopeptides as Grb2-SH2 domain antagonists
    作者:Hilary R Plake、Thomas B Sundberg、Angela R Woodward、Stephen F Martin
    DOI:10.1016/s0040-4039(03)00013-3
    日期:2003.2
    A series of conformationally constrained and flexible pseudopeptide derivatives of the tripeptide pYVN were prepared as potential antagonists of interactions of phosphotyrosine peptides with the Grb2-SH2 domain. The conformation ally constrained compounds contained trans- and cis-cyclopropanes as replacements to enforce locally extended and reverse turn peptide conformations, respectively. (C) 2003 Elsevier Science Ltd. All rights reserved.
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