(R)-N-acetyl-S-(2-aminoethyl)-cysteine | 25528-78-3

• 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: (R)-N-acetyl-S-(2-aminoethyl)-cysteine
• 英文别名: N^α-Acetyl-thialysin；N-acetyl S-2-aminoethylcysteine；(2R)-2-acetamido-3-(2-aminoethylsulfanyl)propanoic acid
• CAS: 25528-78-3
• 化学式: C₇H₁₄N₂O₃S
• 分子量: 206.266
• InChiKey: SXGRUNNIGPMAHW-LURJTMIESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.4
• 重原子数：
  13
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  118
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  二碳酸二叔丁酯 、 (R)-N-acetyl-S-(2-aminoethyl)-cysteine 在 碳酸氢钠 作用下， 以 四氢呋喃 为溶剂， 反应 3.0h， 生成 (R)-N-acetyl-S-<2-(tert-butoxycarbonyl)aminoethyl>-cysteine
  参考文献：
  名称：

  Structural and Conformational Requirements for High-Affinity Binding to the SH2 Domain of Grb2

  摘要：

  Following earlier work on cystine-bridged peptides, cyclic phosphopeptides containing nonreducible mimics of cystine were synthesized that show high affinity and specificity toward the Src homology (SH2) domain of the growth factor receptor-binding protein (Grb2). Replacement of the cystine in the cyclic heptapeptide cyclo(CY*VNVPC) by D-alpha-acetylthialysine or D-alpha-lysine gave cyclo(Y*VNVP(D-alpha-acetyl-thiaK)) (22) and cyclo(Y*VNVP(D-alpha-acetyl-K)) (30), which showed improved binding 10-fold relative to that of the control peptide KPFY*VNVEF (1). NMR spectroscopy and molecular modeling experiments indicate that a beta-turn conformation centered around Y*VNV is essential for high-affinity binding. X-ray structure analyses show that the linear peptide 1 and the cyclic compound 21 adopt a similar binding mode with a beta-turn conformation. Our data confirm the unique structural requirements of the ligand binding site of the SH2 domain of Grb2. Moreover, the potency of our cyclic lactams can be explained by the stabilization of the beta-turn conformation by three intramolecular hydrogen bonds (one mediated by an H2O molecule). These stable and easily accessible cyclic peptides can serve as templates for the evaluation of phosphotyrosine surrogates and further chemical elaboration.

  DOI：

  10.1021/jm9811007
• 作为产物：
  描述：

  乙烯亚胺 、 N-乙酰-L-半胱氨酸 以 乙醇 为溶剂， 生成 (R)-N-acetyl-S-(2-aminoethyl)-cysteine
  参考文献：
  名称：

  Hermann,P. et al., Journal fur praktische Chemie (Leipzig 1954), 1969, vol. 311, p. 1018 - 1028

  摘要：

  DOI：

文献信息

• [EN] METHOD FOR MODIFICATION OF ORGANIC MOLECULES<br/>[FR] PROCÉDÉ DE MODIFICATION DE MOLÉCULES ORGANIQUES
  申请人：UNIV NANYANG TECH

  公开号：WO2012158122A1

  公开（公告）日：2012-11-22

  The present invention is directed to a method of alkylating a thiol group (R-S-H) or seleno group (R-Se-H) in a target molecule wherein the method comprises: reacting a target molecule comprising at least one thiol group with a compound of formula (I) or (II): wherein R is an acetyl group or any other acyl group or is a group comprising any one of: or wherein R in formula (II) can also be an alkyl group; and wherein R' is selected from a group consisting of a hydrogen, a methyl group and an ethyl group.

  本发明涉及一种用于烷基化目标分子中的硫醇基（R-S-H）或硒醇基（R-Se-H）的方法，其中该方法包括：将至少含有一个硫醇基的目标分子与化合物的化合物进行反应（I）或（II）：其中R是乙酰基或任何其他酰基，或是包含以下任何一种的基团：或其中在式（II）中的R也可以是烷基基团；其中R'选自氢、甲基基团和乙基基团组成的一组。
• METHOD FOR MODIFICATION OF ORGANIC MOLECULES
  申请人：Nanyang Technological University

  公开号：EP2707356A1

  公开（公告）日：2014-03-19
• US9309278B2
  申请人：——

  公开号：US9309278B2

  公开（公告）日：2016-04-12
• Hermann,P. et al., Journal fur praktische Chemie (Leipzig 1954), 1969, vol. 311, p. 1018 - 1028
  作者：Hermann,P. et al.

  DOI：——

  日期：——
• Structural and Conformational Requirements for High-Affinity Binding to the SH2 Domain of Grb2
  作者：Peter Ettmayer、Dennis France、John Gounarides、Mark Jarosinski、Mary-Sue Martin、Jean-Michel Rondeau、Michael Sabio、Sid Topiol、Beat Weidmann、Mauro Zurini、Kenneth W. Bair

  DOI：10.1021/jm9811007

  日期：1999.3.1

  Following earlier work on cystine-bridged peptides, cyclic phosphopeptides containing nonreducible mimics of cystine were synthesized that show high affinity and specificity toward the Src homology (SH2) domain of the growth factor receptor-binding protein (Grb2). Replacement of the cystine in the cyclic heptapeptide cyclo(CY*VNVPC) by D-alpha-acetylthialysine or D-alpha-lysine gave cyclo(Y*VNVP(D-alpha-acetyl-thiaK)) (22) and cyclo(Y*VNVP(D-alpha-acetyl-K)) (30), which showed improved binding 10-fold relative to that of the control peptide KPFY*VNVEF (1). NMR spectroscopy and molecular modeling experiments indicate that a beta-turn conformation centered around Y*VNV is essential for high-affinity binding. X-ray structure analyses show that the linear peptide 1 and the cyclic compound 21 adopt a similar binding mode with a beta-turn conformation. Our data confirm the unique structural requirements of the ligand binding site of the SH2 domain of Grb2. Moreover, the potency of our cyclic lactams can be explained by the stabilization of the beta-turn conformation by three intramolecular hydrogen bonds (one mediated by an H2O molecule). These stable and easily accessible cyclic peptides can serve as templates for the evaluation of phosphotyrosine surrogates and further chemical elaboration.