(R)-6-methoxy-α-methyl-2-naphthaleneacetic acid butyl ester

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: (R)-6-methoxy-α-methyl-2-naphthaleneacetic acid butyl ester
• 英文别名: (R)-naproxen n-butyl ester；butyl (2R)-2-(6-methoxynaphthalen-2-yl)propanoate
• 化学式: C₁₈H₂₂O₃
• 分子量: 286.371
• InChiKey: VIKFUEUFSFCFQU-CYBMUJFWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.4
• 重原子数：
  21
• 可旋转键数：
  7
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  35.5
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为产物：
  描述：

  naproxen chloride 在 whole cells of Trichosporon sp 作用下， 以 phosphate buffer 、 二氯甲烷 为溶剂， 反应 96.0h， 生成 (R)-6-methoxy-α-methyl-2-naphthaleneacetic acid butyl ester
  参考文献：
  名称：

  Enzymatic resolution of naproxen

  摘要：

  Trichosporon sp. (TSL), a newly found strain isolated from a locally fermented cottage cheese has been found to be highly stereoselective in the resolution of (S)-(+)-naproxen (ee >99%, Esimilar to500) from the corresponding racemic methyl ester. The process of resolution using whole cells has been scaled up to multi-kg level. Optimization of experimental conditions including downstream processing at 80-100 g/L substrate concentration with >90% recovery has been achieved. Changes in the physical parameters such as the particle size of the substrate play an important role in the resolution kinetics. A new strain of Trichosporon sp. having high cell density in cultivation (>60 g dry cell mass L-1 in 14-16 h) is found to be sufficiently stable for two years in dry powder form at 5-8degreesC. The viability of the resolution process has been further improved by the development of a simple racemization process for the enriched (R)-(-)-ester. (C) 2003 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/s0957-4166(03)00492-0

文献信息

• Improvements of enzyme activity and enantioselectivity in lipase-catalyzed alcoholysis of (R,S)-azolides
  作者：An-Chi Wu、Pei-Yun Wang、Yi-Sheng Lin、Min-Fang Kao、Jin-Ru Chen、Jyun-Fen Ciou、Shau-Wei Tsai

  DOI：10.1016/j.molcatb.2009.11.001

  日期：2010.3

  With Candida antarctica lipase B (CALB)-catalyzed alcoholysis of (R,S)-naproxenyl 1,2,4-triazolide at the optimal conditions (i.e. anhydrous MTBE as the solvent, and methanol as the acyl acceptor at 45 degrees C) as the model system, the enzyme enantioselectivity in terms of V-R/V-S = 105.8 and specific activity for the fast-reacting (R)-azolide V-R/(E-t) = 0.979 mmol/(h g) were greatly improved in comparison with V-R/V-S = 8.0 and V-R/(E-t) = 0.113 mmol/(h g) of using (R,S)-naproxenyl 2,2,2-trifluoroethyl ester as the substrate. The resolution strategy was successfully extended to other (R,S)-profenyl 1,2,4-triazolides and lipases from Candida rugosa (Lipase MY) and Carica papaya (CPL) having opposite enantioselectivity to CALB. Moreover, the kinetic constants were estimated, compared with those obtained via hydrolysis, and employed for modeling time-course conversions of (R,S)-naproxenyl 1,2,4-triazolide in anhydrous MTBE. The advantages of easy substrate preparation, high enzyme reactivity and enantioselectivity, as well as easy product separation from the remaining substrate via reactive extraction demonstrate merits of using (R,S)-azolides but not the corresponding esters for the alcoholytic resolution. (C) 2009 Elsevier B.V. All rights reserved.
• Influence of OR ester group length on the catalytic activity and enantioselectivity of free lipase and immobilized in membrane used for the kinetic resolution of naproxen esters
  作者：L GIORNO、E DAMORE、E DRIOLI、R CASSANO、N PICCI

  DOI：10.1016/j.jcat.2007.01.021

  日期：2007.4.25

  Lipases are suitable catalysts for the kinetic resolution of racemic mixtures due to their ability to discriminate between enantiomers. For this reason, they have been studied largely to develop reactors for the production of optically pure enantiomers. The main problem in these productive systems is enzyme stability and enantiocatalytic selectivity as a function of time. In this work, the enantiocatalytic properties of lipase as a function of the -OR group length were studied. The methyl, butyl, and octyl esters of naproxen were synthesized and used as reagents. The lipase was used as a free agent and immobilized in a polymeric membrane reactor. The results show that selectivity and stability of the enzyme improved while catalytic activity decreased with the -OR length group. The immobilized enzyme had higher activity compared with the free enzyme. (C) 2007 Elsevier Inc. All rights reserved.