N-benzyloxycarbonyl-2(R/S)-trifluoromethylalanine methyl ester | 152604-20-1

• 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: N-benzyloxycarbonyl-2(R/S)-trifluoromethylalanine methyl ester
• 英文别名: Z-(R,S)-(α-trifluoromethyl)Ala-OMe；Z-TFM-Ala-OMe；Methyl 2--3,3,3-trifluoro-2-methylpropanoate；methyl 3,3,3-trifluoro-2-methyl-2-(phenylmethoxycarbonylamino)propanoate
• CAS: 152604-20-1
• 化学式: C₁₃H₁₄F₃NO₄
• 分子量: 305.254
• InChiKey: ZOHPLUHCTQKNDA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.7
• 重原子数：
  21
• 可旋转键数：
  6
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  64.6
• 氢给体数：
  1
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  N-benzyloxycarbonyl-2(R/S)-trifluoromethylalanine methyl ester 在 phosphatbuffer 、 氯甲酸乙酯 、 三乙胺 、 sodium chloride 作用下， 以 二氯甲烷 、 N,N-二甲基甲酰胺 为溶剂， 生成 2-Benzyloxy-4-methyl-4-trifluormethyl-5(4H)-oxazolon
  参考文献：
  名称：

  Untersuchungen zur proteasekatalysierten und chemischen Peptidbindungskn�pfung mit ?-trifluormethylsubstituierten ?-Aminos�uren

  摘要：

  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.

  DOI：

  10.1002/prac.19933350404
• 作为产物：
  描述：

  甲基溴化镁 、 2-benzyloxycarbonylimino-3,3,3-trifluoropropionic acid methyl ester 在 盐酸 作用下， 以 乙醚 、 水 为溶剂， 生成 N-benzyloxycarbonyl-2(R/S)-trifluoromethylalanine 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

文献信息

• Discovery of carboxypeptidase Y as a catalyst for the incorporation of sterically demanding α-fluoroalkyl amino acids into peptides
  作者：Sven Thust、Beate Koksch

  DOI：10.1016/j.tetlet.2003.12.007

  日期：2004.2

  The first example of a direct enzymatic coupling of two different, sterically demanding C-alpha-fluoroalkyl amino acids to amino acid nucleophiles is reported. N-Protected Ala methyl ester derivatives bearing a methyl-, difluoromethyl-, or trifluoromethyl group, respectively, instead of the alpha-proton were accepted as substrates by carboxypeptidase Y and could, therefore, be coupled directly to various nucleophiles. (C) 2003 Published by Elsevier Ltd.
• Burger, Klaus; Schierlinger, Christian; Hollweck, Wolfgang, Liebigs Annalen der Chemie, 1994, # 4, p. 399 - 406
  作者：Burger, Klaus、Schierlinger, Christian、Hollweck, Wolfgang、Muetze, Kerstin

  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.
• 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.