3-{3,5-bis[(bis-pyridin-2-ylmethyl-amino)methyl]-4-hydroxyphenyl}-2-(tert-butoxycarbonylamino)propionic acid methyl ester | 861844-75-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: 3-{3,5-bis[(bis-pyridin-2-ylmethyl-amino)methyl]-4-hydroxyphenyl}-2-(tert-butoxycarbonylamino)propionic acid methyl ester
• 英文别名: Boc-DpaTyr-OMe；methyl (2S)-3-[3,5-bis[[bis(pyridin-2-ylmethyl)amino]methyl]-4-hydroxyphenyl]-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoate
• CAS: 861844-75-9
• 化学式: C₄₁H₄₇N₇O₅
• 分子量: 717.868
• InChiKey: HRNBGQUPTFBFIS-QNGWXLTQSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4
• 重原子数：
  53
• 可旋转键数：
  19
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  143
• 氢给体数：
  2
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  3-{3,5-bis[(bis-pyridin-2-ylmethyl-amino)methyl]-4-hydroxyphenyl}-2-(tert-butoxycarbonylamino)propionic acid methyl ester 在 sodium hydroxide 作用下， 以 甲醇 、 水 为溶剂， 反应 14.0h， 以68%的产率得到3-{3,5-bis[(bis-pyridin-2-ylmethyl-amino)methyl]-4-hydroxyphenyl}-2-(tert-butoxycarbonylamino)propionic acid
  参考文献：
  名称：

  Oligo-Asp Tag/Zn(II) 复合探针作为蛋白质标记和荧光成像的新对

  摘要：

  为了在复杂的生物系统中完成对特定蛋白质的选择性标记，需要掺入蛋白质中的肽标签和互补的小分子探针。尽管已经开发了多种肽标签/探针对作为蛋白质分析的分子工具，但适用于蛋白质实时成像的对的可用性仍然有限。我们现在报告了一个新的肽标签/人工探针对，由可遗传编码的低聚天冬氨酸序列（D4 标签，(D4)n，n = 1-3）和相应的多核 Zn(II) 复合物 (Zn(II)- DpaTyrs）。Zn(II)-DpaTyr 探针与 D4 标签的强结合亲和力是多重配位键和多价效应的结果。用等温滴定量热法定量测定。

  DOI：

  10.1021/ja0618604
• 作为产物：
  描述：

  聚合甲醛 、 N-叔丁氧羰基-L-苯丙氨酸甲酯 、 二甲基吡啶胺 在 盐酸 作用下， 以 乙醇 为溶剂， 反应 36.0h， 以52%的产率得到3-{3,5-bis[(bis-pyridin-2-ylmethyl-amino)methyl]-4-hydroxyphenyl}-2-(tert-butoxycarbonylamino)propionic acid methyl ester
  参考文献：
  名称：

  Solid-phase synthesis of metal-complex containing peptides

  摘要：

  We report the synthesis of Fmoc protected single amino acid chelates (SAAC) and their metal complexes. The modified amino acids are suitable for solid-phase peptide synthesis. The use of 4-hydroxymethylbenzoic acid AM (HMBA-AM) resin allows the nucleophilic cleavage of the peptide-metal complexes from the resin without decomplexation. (c) 2007 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tet.2007.03.147

文献信息

• Oligo-Asp Tag/Zn(II) Complex Probe as a New Pair for Labeling and Fluorescence Imaging of Proteins
  作者：Akio Ojida、Kei Honda、Daisuke Shinmi、Shigeki Kiyonaka、Yasuo Mori、Itaru Hamachi

  DOI：10.1021/ja0618604

  日期：2006.8.1

  specific protein in complicated biological systems, a peptide tag incorporated into the protein and a complementary small molecular probe are required. Although a variety of peptide tag/probe pairs have been developed as molecular tools for protein analyses, the availability of pairs suitable for real-time imaging of proteins is still limited. We now report a new peptide tag/artificial probe pair composed

  为了在复杂的生物系统中完成对特定蛋白质的选择性标记，需要掺入蛋白质中的肽标签和互补的小分子探针。尽管已经开发了多种肽标签/探针对作为蛋白质分析的分子工具，但适用于蛋白质实时成像的对的可用性仍然有限。我们现在报告了一个新的肽标签/人工探针对，由可遗传编码的低聚天冬氨酸序列（D4 标签，(D4)n，n = 1-3）和相应的多核 Zn(II) 复合物 (Zn(II)- DpaTyrs）。Zn(II)-DpaTyr 探针与 D4 标签的强结合亲和力是多重配位键和多价效应的结果。用等温滴定量热法定量测定。
• Ratiometric fluorescence detection of a tag fused protein using the dual-emission artificial molecular probe
  作者：Kei Honda、Eiji Nakata、Akio Ojida、Itaru Hamachi

  DOI：10.1039/b608684e

  日期：——

  We have successfully developed a ratiometric detection system for protein of interest using the complementary recognition pair of the tetra-aspartate peptide tag and the SNARF-appended Zn(II)–DpaTyr probe.

  我们利用四天冬氨酸肽标签和 SNARF 应用 Zn(II)-DpaTyr 探针的互补识别对，成功开发了一种相关蛋白质的比率检测系统。
• Anion-Mediated Phase Transfer of Zinc(II)-Coordinated Tyrosine Derivatives
  作者：Hua Jiang、Edward J. O'Neil、Kristy M. DiVittorio、Bradley D. Smith

  DOI：10.1021/ol0510421

  日期：2005.7.1

  Tyrosine-derived Zn2+ coordination complexes and their fluorescent NBD conjugates are synthesized in a short, high-yielding procedure. The Zn2+ complexes are highly water soluble, but in the presence of sodium laurate they readily transfer into an octanol layer. Furthermore, the NBD-labeled bis-Zn2+ complex can partition into vesicle membranes containing anionic phospholipids.
• Specific Enrichment of Phosphoproteins Using Functionalized Multivalent Nanoparticles
  作者：Leekyoung Hwang、Serife Ayaz-Guner、Zachery R. Gregorich、Wenxuan Cai、Santosh G. Valeja、Song Jin、Ying Ge

  DOI：10.1021/ja511833y

  日期：2015.2.25

  Analysis of protein phosphorylation remains a significant challenge due to the low abundance of phosphoproteins and the low stoichiometry of phosphorylation, which requires effective enrichment of phosphoproteins. Here we have developed superparamagnetic nanoparticles (NPs) whose surface is functionalized by multivalent ligand molecules that specifically bind to the phosphate groups on any phosphoproteins. These NPs enrich phosphoproteins from complex cell and tissue lysates with high specificity as confirmed by SDS-PAGE analysis with a phosphoprotein-specific stain and mass spectrometry analysis of the enriched phosphoproteins. This method enables universal and effective capture, enrichment, and detection of intact phosphoproteins toward a comprehensive analysis of the phosphoproteome.
• Solid-phase synthesis of metal-complex containing peptides
  作者：Georg Dirscherl、Robert Knape、Paul Hanson、Burkhard König

  DOI：10.1016/j.tet.2007.03.147

  日期：2007.6

  We report the synthesis of Fmoc protected single amino acid chelates (SAAC) and their metal complexes. The modified amino acids are suitable for solid-phase peptide synthesis. The use of 4-hydroxymethylbenzoic acid AM (HMBA-AM) resin allows the nucleophilic cleavage of the peptide-metal complexes from the resin without decomplexation. (c) 2007 Elsevier Ltd. All rights reserved.