2,2-diethyl-N-(trifluoroacetyl)glycine | 84310-99-6

• 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: 2,2-diethyl-N-(trifluoroacetyl)glycine
• 英文别名: 2-Ethyl-2-(2,2,2-trifluoroacetamido)butanoic acid；2-ethyl-2-[(2,2,2-trifluoroacetyl)amino]butanoic acid
• CAS: 84310-99-6
• 化学式: C₈H₁₂F₃NO₃
• 分子量: 227.183
• InChiKey: ACLAGRMMFRNIQY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.9
• 重原子数：
  15
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  66.4
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  2,2-diethyl-N-(trifluoroacetyl)glycine 在 氯化亚砜 作用下， 以 乙腈 为溶剂， 反应 101.0h， 生成 ethyl 2-ethyl-2-<<2-ethyl-1-oxo-2-<(trifluoroacetyl)amino>butyl>amino>butanoate
  参考文献：
  名称：

  Helicalversus Planar Conformation of Homooligopeptides Prepared from Diethylglycine (=2-Amino-2-ethylbutanoic Acid)

  摘要：

  Homooligopeptides containing alpha,alpha-diethylgycine (= 2-amino-2-ethylbutanoic acid), were synthesized by conventional solution methods. An ethyl or methyl ester was used as protecting group at the C-terminus and a trifluoroacetyl group as protecting group at the N-terminus of the peptides. The conformations of such tri-, penta-, and hexapeptides in the solid stare were studied using X-ray crystallographic analysis, and were shown to be a bent planar CS-conformation in the case of tripeptide 8a, and a 3(10)-helical structure in the case of pentapeptide 10 and hexapeptide 11. IR and H-1-NMR spectra revealed that the dominant conformation of hexapeptide 11 in CDCl3 solution was not the 3(10)-helical structure shown in the solid state, but a fully planar C5 structure.

  DOI：

  10.1002/(sici)1522-2675(19990407)82:4<494::aid-hlca494>3.0.co;2-a
• 作为产物：
  描述：

  1-氨基-1-乙基丙基氰化物 在 盐酸 作用下， 反应 192.0h， 生成 2,2-diethyl-N-(trifluoroacetyl)glycine
  参考文献：
  名称：

  Helicalversus Planar Conformation of Homooligopeptides Prepared from Diethylglycine (=2-Amino-2-ethylbutanoic Acid)

  摘要：

  Homooligopeptides containing alpha,alpha-diethylgycine (= 2-amino-2-ethylbutanoic acid), were synthesized by conventional solution methods. An ethyl or methyl ester was used as protecting group at the C-terminus and a trifluoroacetyl group as protecting group at the N-terminus of the peptides. The conformations of such tri-, penta-, and hexapeptides in the solid stare were studied using X-ray crystallographic analysis, and were shown to be a bent planar CS-conformation in the case of tripeptide 8a, and a 3(10)-helical structure in the case of pentapeptide 10 and hexapeptide 11. IR and H-1-NMR spectra revealed that the dominant conformation of hexapeptide 11 in CDCl3 solution was not the 3(10)-helical structure shown in the solid state, but a fully planar C5 structure.

  DOI：

  10.1002/(sici)1522-2675(19990407)82:4<494::aid-hlca494>3.0.co;2-a

文献信息

• The 2.0 ₅ ‐helix in hetero‐oligopeptides entirely composed of C ^α,α ‐disubstituted glycines with both side chains longer than methyls
  作者：Marco Crisma、Cristina Peggion、Alessandro Moretto、Raja Banerjee、Subhrangshu Supakar、Fernando Formaggio、Claudio Toniolo

  DOI：10.1002/bip.22450

  日期：2014.3

  consecutive fully‐extended conformation (2.05‐helix) has been already clearly demonstrated in homo‐oligopeptides based on quaternary α‐amino acids with both side chains longer than methyls, but not cyclized on the α‐carbon atom. To extend the scope of this research, in this work we investigated the occurrence of this flat 3D‐structure in hetero‐oligopeptides, each composed of two or three different residues of

  非常罕见但可能非常有趣的多重连续完全延伸构象（2.05 螺旋）的存在已经在基于双侧链长于甲基的四元 α-氨基酸的同源寡肽中得到清楚证明，但不是在α-碳原子上环化。为了扩展这项研究的范围，在这项工作中，我们研究了这种扁平 3D 结构在异寡肽中的出现，每个异寡肽由该类别的两个或三个不同的残基组成。末端保护的肽系列合成到四肽水平是通过溶液方法进行的。对所得低聚物进行化学和构象表征。获得的数据表明CDCl3 中完全扩展的构象占绝大多数。然而，在 CD3CN 中观察到溶剂驱动转变为主要的 310 螺旋结构。这两种构象之间微妙的局部平衡被证实在结晶状态下发生。即使从 310 螺旋结构开始，CHCl3 中异四肽的分子动力学模拟也收敛到完全延伸的构象。© 2013 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 145–158, 2014。
• An Extended Planar C5 Conformation and a 310-Helical Structure of Peptide Foldamer Composed of Diverse -Ethylated ,-Disubstituted -Amino Acids
  作者：Masakazu Tanaka、Shin Nishimura、Makoto Oba、Yosuke Demizu、Masaaki Kurihara、Hiroshi Suemune

  DOI：10.1002/chem.200204476

  日期：2003.7.7

  active peptide foldamers Tfa-[(S)-(alphaEt)Leu]-[(S)-(alphaEt)Nva]-Deg-[(S)-(alphaEt)Nle]-OEt (10) and Tfa-[(S)-(alphaEt)Val]-[(S)-(alphaEt)Leu]-[(S)-(alphaEt)Nva]-Deg-[(S)-(alphaEt)Nl e]-OEt (11) composed of diverse alpha-ethylated alpha,alpha-disubstituted alpha-amino acids were synthesized. The dominant conformation of these peptides in solution was an unusual, fully extended planar conformation, and

  光学活性肽折叠剂Tfa-[（S）-（alphaEt）Leu]-[（S-（alphaEt）Nva] -Deg-[（S）-（alphaEt）Nle] -OEt（10）和Tfa-[（ S）-（alphaEt）Val]-[（S）-（alphaEt）Leu]-[（S）-（alphaEt）Nva] -Deg-[（S）-（alphaEt）Nle e] -OEt（11）组成合成了多种α-乙基化的α，α-二取代的α-氨基酸。这些肽在溶液中的主要构象是一个不寻常的，完全延伸的平面构象，并且在晶体状态下是右旋（P）和左旋（M）3（10）螺旋结构，其中10和P图11中的3（10）-螺旋结构。由手性α-乙基化的α，α-二取代的α-氨基酸制备的肽的优选平面C（5）构象与由手性α-甲基化的α，制备的肽的3（10）-螺旋结构完全不同，
• Helicalversus Planar Conformation of Homooligopeptides Prepared from Diethylglycine (=2-Amino-2-ethylbutanoic Acid)
  作者：Masakazu Tanaka、Naoto Imawaka、Masaaki Kurihara、Hiroshi Suemune

  DOI：10.1002/(sici)1522-2675(19990407)82:4<494::aid-hlca494>3.0.co;2-a

  日期：1999.4.7

  Homooligopeptides containing alpha,alpha-diethylgycine (= 2-amino-2-ethylbutanoic acid), were synthesized by conventional solution methods. An ethyl or methyl ester was used as protecting group at the C-terminus and a trifluoroacetyl group as protecting group at the N-terminus of the peptides. The conformations of such tri-, penta-, and hexapeptides in the solid stare were studied using X-ray crystallographic analysis, and were shown to be a bent planar CS-conformation in the case of tripeptide 8a, and a 3(10)-helical structure in the case of pentapeptide 10 and hexapeptide 11. IR and H-1-NMR spectra revealed that the dominant conformation of hexapeptide 11 in CDCl3 solution was not the 3(10)-helical structure shown in the solid state, but a fully planar C5 structure.