(R)-1,2-bis(3,5-dimethoxyphenyl)-2-hydroxyethanone | 1107608-83-2

• 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: (R)-1,2-bis(3,5-dimethoxyphenyl)-2-hydroxyethanone
• 英文别名: TMBZ；(R)-3,3',5,5'-tetramethoxy benzoin；TMB；r-3,3',5,5'-Tetramethoxybenzoin；(2R)-1,2-bis(3,5-dimethoxyphenyl)-2-hydroxyethanone
• CAS: 1107608-83-2
• 化学式: C₁₈H₂₀O₆
• 分子量: 332.353
• InChiKey: FRFNNKFPADJNFG-QGZVFWFLSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  None
• 重原子数：
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• 可旋转键数：
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• 环数：
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• sp3杂化的碳原子比例：
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• 拓扑面积：
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• 氢给体数：
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• 氢受体数：
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反应信息

• 作为反应物：
  描述：

  (R)-1,2-bis(3,5-dimethoxyphenyl)-2-hydroxyethanone 在 哌啶 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 H-Rink amide ChemMatrix resin
  参考文献：
  名称：

  Synthesis and evaluation of phosphopeptides containing iminodiacetate groups as binding ligands of the Src SH2 domain

  摘要：

  Phosphopeptide pTyr-Glu-Glu-Ile (pYEEI) has been introduced as an optimal Src SH2 domain ligand. Peptides, Ac-K(IDA)pYEEIEK(IDA) (1), Ac-KpYEEIEK (2), Ac-K(IDA) pYEEIEK (3), and Ac-KpYEEIEK(IDA) (4), containing 0-2 iminodiacetate (IDA) groups at the N- and C-terminal lysine residues were synthesized and evaluated as the Src SH2 domain binding ligands. Fluorescence polarization assays showed that peptide 1 had a higher binding affinity (K-d = 0.6 mu M) to the Src SH2 domain when compared with Ac-pYEEI (K-d = 1.7 mu M), an optimal Src SH2 domain ligand, and peptides 2-4 (K-d = 2.9-52.7 mu M). The binding affinity of peptide 1 to the SH2 domain was reduced by more than 2-fold (K-d = 1.6 mu M) upon addition of Ni2+ (300 mu M), possibly due to modest structural effect of Ni2+ on the protein as shown by circular dichroism experimental results. The binding affinity of 1 was restored in the presence of EDTA (300 mu M) (K-d = 0.79 mu M). These studies suggest that peptides containing IDA groups may be used for designing novel SH2 domain binding ligands. (C) 2009 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.bioorg.2009.05.003
• 作为产物：
  描述：

  3,5-二甲氧基苯甲醛 在 benzoin aldolase 、 焦磷酸硫胺素 、 magnesium chloride 作用下， 以 水 、 二甲基亚砜 为溶剂， 生成 (R)-1,2-bis(3,5-dimethoxyphenyl)-2-hydroxyethanone
  参考文献：
  名称：

  Biochemical peculiarities of benzaldehyde lyase from Pseudomonas fluorescens Biovar I in the dependency on pH and cosolvent concentration

  摘要：

  Benzaldehyde lyase from Pseudomonas fluorescens (BAL, EC 4.1.2.38) is a versatile catalyst for stereoselective carboligations. Nevertheless, rather inconsistent data about its biochemical properties are reported in literature. In this study, the dependency of BAL activity on ionic strength, pH, and concentration of DMSO was for the first time systematically investigated and interpreted. It was found that the activity of BAL strongly depends on all three parameters, and a correlation exists between the dependency on pH and DMSO concentration. This correlation could be explained by an interaction of DMSO with an ionic amino acid in the catalytic site. A model-based analysis indicated that the pK(a) of this residue shifts to the alkaline milieu upon addition of DMSO. Consequently, the optimum pH also shifts to alkaline values when DMSO is present. Potentiometric experiments confirmed that the pK(a) can most probably be attributed to Glu50 which governs the activity increase of BAL on the acidic limb of its pH-activity profile. With these findings, the apparently contradicting data from literature become comprehensible and optimal reaction conditions for synthesis can easily be deduced. (C) 2009 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.bioorg.2009.03.001

文献信息

• Systematic assessment of the stability of benzaldehyde lyase in aqueous–organic biphasic systems and its stabilization by modification with methoxy-poly(ethylene) glycol
  作者：Anne van den Wittenboer、Bernd Niemeijer、Sanjib Kumar Karmee、Marion B. Ansorge-Schumacher

  DOI：10.1016/j.molcatb.2010.08.007

  日期：2010.12

  Benzaldehyde lyase from Pseudomonas fluorescens Biovar I [BAL; E.C.4.1.2.38] catalyzes the stereoselective formation of C-C bonds coupling aldehydes to generate alpha-hydroxy ketones. A broad range of poorly water-soluble substrates are accepted in forward and reverse reactions. In this study, the stability of BAL in aqueous-organic biphasic systems as promising reaction media was systematically investigated using methyl-tert-butylether, 2-octanone, and toluene as the organic phase. Surprisingly, a strong individual molecular toxicity of these water-immiscible solvents was observed along with the interfacial toxicity exerted by the aqueous-organic interfaces. They could be considerably reduced by covalent attachment of methoxy-poly(ethylene) glycol (mPEG(750) and mPEG(2000)) to the enzyme surface increasing the half-life by a factor of up to 18. However, under reactive conditions solvent effects were strongly superimposed by an additional deactivating effect, possibly caused by the aldehyde substrate, and no differences between unmodified and modified BAL were detectable. For technical application of the enzyme in aqueous-organic biphasic media additional strategies for stabilization will therefore be desirable. (C) 2010 Elsevier B.V. All rights reserved.