香兰素13C6 | 201595-58-6

• 分子结构分类: 有机化合物 - 苯类化合物 - 酚类
• 中文名称: 香兰素13C6
• 中文别名: 香兰素
• 英文名称: (ring-13C6)vanillin
• 英文别名: vanillin-¹³C₆；Vanillin-13C6；4-hydroxy-3-methoxy(1,2,3,4,5,6-13C6)cyclohexa-1,3,5-triene-1-carbaldehyde
• CAS: 201595-58-6
• 化学式: C₈H₈O₃
• 分子量: 158.084
• InChiKey: MWOOGOJBHIARFG-BOCFXHSMSA-N

物化性质

• 熔点：
  81 - 83°C
• 溶解度：
  可溶于氯仿（少许）、乙酸乙酯（少许）、甲醇（少许）

计算性质

• 辛醇/水分配系数(LogP)：
  1.2
• 重原子数：
  11
• 可旋转键数：
  2
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  46.5
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  香兰素13C6 在 吡啶 、 三(3,6-二氧杂庚基)胺 、 potassium carbonate 作用下， 以 二氯甲烷 为溶剂， 反应 13.0h， 生成 (ring-13C6)-E-3-(4-acetoxy-3-methoxyphenyl)-2-propenal
  参考文献：
  名称：

  针叶树中的松柏醇代谢——II。松柏醇和二氢松柏醇生物合成

  摘要：

  松柏醛和 NADPH 当与从松树的木质部发育中分离的微粒体一起孵育时，在体外产生松柏醇和二氢松柏醇。还发现 D-(+)-Pinitol 是微粒体成分。使用环-(13)C(6)-松柏基通过同位素稀释联合气相色谱质谱 (GC/MS) 对松柏和松柏的休眠芽、形成层、树皮和针叶中的内源 E-松柏醇含量进行定量酒精的水平与内源性吲哚 3-基乙酸 (IAA) 相似。伤口（分支环剥）导致休眠的非木质化形成层中内源性 E-松柏醇的含量增加了 10 倍以上，这清楚地表明单木质醇生物合成与木质化无关。

  DOI：

  10.1016/s0031-9422(01)00142-x

文献信息

• Optimized synthesis of four isotopically labeled(13C-enriched) phenolic acids via a malonic acid condensation
  作者：Rebecca J. Robbins、Walter F. Schmidt

  DOI：10.1002/jlcr.869

  日期：2004.10.15

  Four isotopically (13C)-labeled phenolic acids (caffeic [M + 3], sinapic [M + 2], p-coumaric [M + 6] and ferulic [M + 6] acids) were synthesized via a simple one-step malonic acid condensation with a series of aldehydes. The aldehydes and the malonic acid were variously labeled and unlabeled to vary the enriched sites. 13C and 1H NMR analyses together confirmed the labeled positions. LC/MS confirmed the masses. These acids are intended for use as internal standards for isotope dilution mass spectrometry (IDMS). Copyright © 2004 John Wiley & Sons, Ltd. (1)

  四种同位素（13C）标记的酚酸（咖啡酸[M + 3]、山奈酸[M + 2]、对香豆酸[M + 6]和阿魏酸[M + 6]）是通过简单的丙二酸与一系列醛缩合一步合成的。为了改变富集位点，对醛和丙二酸进行了不同的标记和非标记。13C 和 1H NMR 分析共同证实了标记的位置。LC/MS 确认了质量。这些酸可用作同位素稀释质谱法 (IDMS) 的内部标准。Copyright © 2004 John Wiley & Sons, Ltd. All Rights Reserved. (1)
• Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid β-protein fibrils
  作者：Yuichi Masuda、Masashi Fukuchi、Tatsuya Yatagawa、Masato Tada、Kazuyuki Takeda、Kazuhiro Irie、Ken-ichi Akagi、Youko Monobe、Takayoshi Imazawa、K. Takegoshi

  DOI：10.1016/j.bmc.2011.08.052

  日期：2011.10

  Aggregation of 42-residue amyloid beta-protein (A beta 42) plays a pivotal role in the etiology of Alzheimer's disease (AD). Curcumin, the yellow pigment in the rhizome of turmeric, attracts considerable attention as a food component potentially preventing the pathogenesis of AD. This is because curcumin not only inhibits the aggregation of A beta 42 but also binds to its aggregates (fibrils), resulting in disaggregation. However, the mechanism of interaction between curcumin and the A beta 42 fibrils remains unclear. In this study, we analyzed the binding mode of curcumin to the A beta 42 fibrils by solid-state NMR using dipolar-assisted rotational resonance (DARR). To improve the quality of 2D spectra, 2D DARR data were processed with the covariance NMR method, which enabled us to detect weak cross peaks between carbons of curcumin and those of the A beta 42 fibrils. The observed C-13-C-13 cross peaks indicated that curcumin interacts with the 12th and 17-21st residues included in the beta-sheet structure in the A beta 42 fibrils. Interestingly, aromatic carbons adjacent to the methoxy and/or hydroxy groups of curcumin showed clear cross peaks with the A beta 42 fibrils. This suggested that these functional groups of curcumin play an important role in its interaction with the A beta 42 fibrils. (C) 2011 Elsevier Ltd. All rights reserved.