(2R,3R)-1-(N-tert-butoxycarbonyl)amino-2,3-diphenyl-1-cyclopropanecarboxylic acid | 214492-28-1

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 二苯乙烯类
• 英文名称: (2R,3R)-1-(N-tert-butoxycarbonyl)amino-2,3-diphenyl-1-cyclopropanecarboxylic acid
• 英文别名: (2R,3R)-1-[(2-methylpropan-2-yl)oxycarbonylamino]-2,3-diphenylcyclopropane-1-carboxylic acid
• CAS: 214492-28-1
• 化学式: C₂₁H₂₃NO₄
• 分子量: 353.418
• InChiKey: UBMCDYPPLGQSRJ-IRXDYDNUSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.7
• 重原子数：
  26
• 可旋转键数：
  6
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  75.6
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  (2R,3R)-1-(N-tert-butoxycarbonyl)amino-2,3-diphenyl-1-cyclopropanecarboxylic acid 在 盐酸 、 N-羟基-7-氮杂苯并三氮唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 二氯甲烷 、 乙酸乙酯 为溶剂， 反应 198.58h， 生成 {(2R,3R)-1-[(2R,3R)-1-((2R,3R)-1-Isopropylcarbamoyl-2,3-diphenyl-cyclopropylcarbamoyl)-2,3-diphenyl-cyclopropylcarbamoyl]-2,3-diphenyl-cyclopropyl}-carbamic acid tert-butyl ester
  参考文献：
  名称：

  Turn and Helical Peptide Handedness Governed Exclusively by Side-Chain Chiral Centers

  摘要：

  We have examined the preferred 3D structure of homopeptides based on an alpha-amino acid lacking the asymmetry at the alpha-carbon but exhibiting chirality in the side chains (at the two beta-carbons). These joint stereochemical properties are remarkably unusual for an alpha-amino acid. To this end, we carried out an experimental investigation by X-ray diffraction and NMR spectrometry. The results point to a well-defined relationship between screw sense of the turn and helix structures formed and side-chain configurations.

  DOI：

  10.1021/ja043116u
• 作为产物：
  描述：

  (R,R)-(+)-4,5-diphenyl-1,3,2-dioxathiolan-2-one 在 ruthenium trichloride 、 sodium hydroxide 、 sodium periodate 、 二苯基膦叠氮化物 、 sodium hydride 、 三乙胺 作用下， 以 甲醇 、 四氯化碳 、 氯磺酸 、 乙腈 为溶剂， 反应 81.0h， 生成 (2R,3R)-1-(N-tert-butoxycarbonyl)amino-2,3-diphenyl-1-cyclopropanecarboxylic acid
  参考文献：
  名称：

  Conformational Preferences of RNase A C-Peptide Derivatives Containing a Highly Constrained Analogue of Phenylalanine

  摘要：

  Both enantiomers of a highly constrained derivative of phenylalanine, FiFi, were prepared in optically pure form. Studies were performed to elucidate the effects of substituting this amino acid for phenylalanine in RN-24, a derivative of the RNase A C-peptide. Thus RN-24, and the analogues 9 and 10, in which Phe-8 was replaced by each of the enantiomers of FiFi, were prepared. Comparative circular dichroism (CD) experiments indicated relative tendencies to adopt helical structures, and variable-temperature CD studies showed the relative ease with which these conformations were lost at elevated temperatures. These observations were rationalized via computer-assisted molecular modeling, which showed that the phenyl groups of (R,R)-FiFi in the peptidomimetic 9 can be accommodated via distortion of the helical conformations and that such distorted conformations persist as the temperature is increased. Conversely, intolerable contacts occur in an analogous conformation of the (S,S)-FiFi peptidomimetic 10 and these preclude helicity. Consistent with these observations, molecular dynamics studies of these peptidomimetics at 276 K indicate that helical conformations of 9 and RN-24 are observable under conditions in which the analogous conformation of 10 is lost. Overall, these studies demonstrate that cyclopropane amino acids can be used to enforce elements of secondary structure (albeit distorted) or to preclude them altogether.

  DOI：

  10.1021/ja981153d

文献信息

• Facile synthesis and highly efficient resolution of a constrained cyclopropane analogue of phenylalanine
  作者：Ana I Jiménez、Pilar López、Laureano Oliveros、Carlos Cativiela

  DOI：10.1016/s0040-4020(01)00530-0

  日期：2001.7

  Enantiomerically pure (2R,3R)- and (2S,3S)-1-(N-tert-butoxycarbonyl)amino-2,3-diphenl-1-cyclopropanecarboxylic acids have been prepared by HPLC resolution of a racemic precursor. The complete stereoselectivity of the cyclopropanation process, together with the high efficiency of the subsequent transformations and the: chromatographic resolution, allowed the preparation of optically pure compounds on a multigram scale. (C) 2001 Elsevier Science Ltd. All rights reserved.
• Conformational Preferences of RNase A <i>C</i>-Peptide Derivatives Containing a Highly Constrained Analogue of Phenylalanine
  作者：Destardi Moye-Sherman、Song Jin、Inhye Ham、Dongyeol Lim、J. Martin Scholtz、Kevin Burgess

  DOI：10.1021/ja981153d

  日期：1998.9.1

  Both enantiomers of a highly constrained derivative of phenylalanine, FiFi, were prepared in optically pure form. Studies were performed to elucidate the effects of substituting this amino acid for phenylalanine in RN-24, a derivative of the RNase A C-peptide. Thus RN-24, and the analogues 9 and 10, in which Phe-8 was replaced by each of the enantiomers of FiFi, were prepared. Comparative circular dichroism (CD) experiments indicated relative tendencies to adopt helical structures, and variable-temperature CD studies showed the relative ease with which these conformations were lost at elevated temperatures. These observations were rationalized via computer-assisted molecular modeling, which showed that the phenyl groups of (R,R)-FiFi in the peptidomimetic 9 can be accommodated via distortion of the helical conformations and that such distorted conformations persist as the temperature is increased. Conversely, intolerable contacts occur in an analogous conformation of the (S,S)-FiFi peptidomimetic 10 and these preclude helicity. Consistent with these observations, molecular dynamics studies of these peptidomimetics at 276 K indicate that helical conformations of 9 and RN-24 are observable under conditions in which the analogous conformation of 10 is lost. Overall, these studies demonstrate that cyclopropane amino acids can be used to enforce elements of secondary structure (albeit distorted) or to preclude them altogether.
• Turn and Helical Peptide Handedness Governed Exclusively by Side-Chain Chiral Centers
  作者：Soledad Royo、Wim M. De Borggraeve、Cristina Peggion、Fernando Formaggio、Marco Crisma、Ana I. Jiménez、Carlos Cativiela、Claudio Toniolo

  DOI：10.1021/ja043116u

  日期：2005.2.1

  We have examined the preferred 3D structure of homopeptides based on an alpha-amino acid lacking the asymmetry at the alpha-carbon but exhibiting chirality in the side chains (at the two beta-carbons). These joint stereochemical properties are remarkably unusual for an alpha-amino acid. To this end, we carried out an experimental investigation by X-ray diffraction and NMR spectrometry. The results point to a well-defined relationship between screw sense of the turn and helix structures formed and side-chain configurations.