Methyl 2-Benzoxycarbonylamino-3,3,3-trifluoro-2-hydroxypropionate | 129398-24-9

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: Methyl 2-Benzoxycarbonylamino-3,3,3-trifluoro-2-hydroxypropionate
• 英文别名: Z-TFM-Gly(OH)-OMe；2-benzyloxycarbonylamino-3,3,3-trifluoro-2-hydroxypropionic acid methyl ester；Propionic acid, 2-benzyloxycarbonylamino-3,3,3-trifluoro-2-hydroxy-, methyl ester；methyl 3,3,3-trifluoro-2-hydroxy-2-(phenylmethoxycarbonylamino)propanoate
• CAS: 129398-24-9
• 化学式: C₁₂H₁₂F₃NO₅
• 分子量: 307.226
• InChiKey: MOLRVRSQBNZTTO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.7
• 重原子数：
  21
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.33
• 拓扑面积：
  84.9
• 氢给体数：
  2
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  Methyl 2-Benzoxycarbonylamino-3,3,3-trifluoro-2-hydroxypropionate 在 三氟乙酸酐 、 吡啶 作用下， 以 乙醚 为溶剂， 反应 4.0h， 生成 2-benzyloxycarbonylimino-3,3,3-trifluoropropionic acid methyl ester
  参考文献：
  名称：

  Chemical Labeling Strategy with (R)- and (S)-Trifluoromethylalanine for Solid State ¹⁹F NMR Analysis of Peptaibols in Membranes

  摘要：

  Substitution of a single Aib-residue in a peptaibol with (R)- and (S)-trifluoromethylalanine yields two local orientational constraints theta by solid state F-19 NMR. The structure of the membrane-perturbing antibiotic alamethicin in DMPC bilayers was analyzed in terms of two angles tau and rho from six such constraints, showing that the N-terminus (up to a kink at Pro14) is folded as an alpha-helix, tilted away from the membrane normal by 8 degrees, and assembled as an oligomer. The new F-19 NMR label CF3-Ala has thus been demonstrated to be highly sensitive, virtually unperturbing, and ideally suited to characterize peptaibols in membranes.

  DOI：

  10.1021/ja9067595
• 作为产物：
  描述：

  三氟丙酮酸甲酯 、 氨基甲酸苄酯 以 二氯甲烷 为溶剂， 以93%的产率得到Methyl 2-Benzoxycarbonylamino-3,3,3-trifluoro-2-hydroxypropionate
  参考文献：
  名称：

  Chemical Labeling Strategy with (R)- and (S)-Trifluoromethylalanine for Solid State ¹⁹F NMR Analysis of Peptaibols in Membranes

  摘要：

  Substitution of a single Aib-residue in a peptaibol with (R)- and (S)-trifluoromethylalanine yields two local orientational constraints theta by solid state F-19 NMR. The structure of the membrane-perturbing antibiotic alamethicin in DMPC bilayers was analyzed in terms of two angles tau and rho from six such constraints, showing that the N-terminus (up to a kink at Pro14) is folded as an alpha-helix, tilted away from the membrane normal by 8 degrees, and assembled as an oligomer. The new F-19 NMR label CF3-Ala has thus been demonstrated to be highly sensitive, virtually unperturbing, and ideally suited to characterize peptaibols in membranes.

  DOI：

  10.1021/ja9067595

文献信息

• Burger, Klaus; Hoess, Eva; Gaa, Karl, Zeitschrift fur Naturforschung, B: Chemical Sciences, 1991, vol. 46, # 3, p. 361 - 384
  作者：Burger, Klaus、Hoess, Eva、Gaa, Karl、Sewald, Norbert、Schierlinger, Christian

  DOI：——

  日期：——
• Untersuchungen zur proteasekatalysierten und chemischen Peptidbindungskn�pfung mit ?-trifluormethylsubstituierten ?-Aminos�uren
  作者：K. Burger、Kerstin M�tze、Wolfgang Hollweck、Beate Koksch、Peter Kuhl、H.-D. Jakubke、J�rgen Riede、Annette Schier

  DOI：10.1002/prac.19933350404

  日期：——

  Subtilisin, alpha-chymotrypsin and papain catalyzed hydrolyses of alpha-trifluoromethyl substituted N-benzyloxycarbonyl amino acid methylesters (Z-TFM-Xaa-OMe) 1 can be achieved only in the case of 3,3,3-trifluoroalanine. Enzymatic incorporation of Z-TFM amino acids 2 into N-terminal position of dipeptides also fails. In contrary, dipeptides with a TFM amino acid moiety in N-terminal position, e. g. TFM-Phg-L-Phe-OMe 5, react with H-Leu-NH2 to give the corresponding tripeptides 6 in high yield. Z protected dipeptide derivatives 8 with N-terminal TFM amino acids can be obtained via 4-trifluoromethyl-5-(4H)-oxazolones 7.
• BURGER, KLAUS;HOSS. , EVA;GAA, KARL;SEWALD, NORBERT;SCHIERLINGER, CHRISTI+, Z. NATURFORSCH. B , 46,(1991) N, C. 361-384
  作者：BURGER, KLAUS、HOSS. , EVA、GAA, KARL、SEWALD, NORBERT、SCHIERLINGER, CHRISTI+

  DOI：——

  日期：——
• Chemical Labeling Strategy with (<i>R</i>)- and (<i>S</i>)-Trifluoromethylalanine for Solid State ¹⁹F NMR Analysis of Peptaibols in Membranes
  作者：Daniel Maisch、Parvesh Wadhwani、Sergii Afonin、Christoph Böttcher、Beate Koksch、Anne S. Ulrich

  DOI：10.1021/ja9067595

  日期：2009.11.4

  Substitution of a single Aib-residue in a peptaibol with (R)- and (S)-trifluoromethylalanine yields two local orientational constraints theta by solid state F-19 NMR. The structure of the membrane-perturbing antibiotic alamethicin in DMPC bilayers was analyzed in terms of two angles tau and rho from six such constraints, showing that the N-terminus (up to a kink at Pro14) is folded as an alpha-helix, tilted away from the membrane normal by 8 degrees, and assembled as an oligomer. The new F-19 NMR label CF3-Ala has thus been demonstrated to be highly sensitive, virtually unperturbing, and ideally suited to characterize peptaibols in membranes.