L-N-tert-butoxycarbonyl-2-naphthylalanine cyanomethyl ester

• 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: L-N-tert-butoxycarbonyl-2-naphthylalanine cyanomethyl ester
• 英文别名: (S)-cyanomethyl 2-((tert-butoxycarbonyl)amino)-3-(naphthalen-2-yl)propanoate；Boc-Nap-OCH2CN；cyanomethyl (2S)-2-[(2-methylpropan-2-yl)oxycarbonylamino]-3-naphthalen-2-ylpropanoate
• 化学式: C₂₀H₂₂N₂O₄
• 分子量: 354.406
• InChiKey: WSIJQHSEAPCKCT-KRWDZBQOSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  26
• 可旋转键数：
  8
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.35
• 拓扑面积：
  88.4
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  L-N-tert-butoxycarbonyl-2-naphthylalanine cyanomethyl ester 在 三异丙基硅烷 、 四丁基醋酸铵 、 三氟乙酸 作用下， 以 四氢呋喃 为溶剂， 反应 48.0h， 生成 (S)-(2R,3R,4R,5R)-2-(6-amino-9H-purin-9-yl)-4-hydroxy-5-(hydroxymethyl)tetrahydrofuran-3-yl 2-amino-3-(naphthalen-2-yl)propanoate
  参考文献：
  名称：

  N-Terminal Protein Modification Using Simple Aminoacyl Transferase Substrates

  摘要：

  Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.

  DOI：

  10.1021/ja2055098
• 作为产物：
  描述：

  Boc-3-(2-萘基)-L-丙氨酸 、 氯乙腈 在 N,N-二异丙基乙胺 作用下， 反应 12.0h， 以99%的产率得到L-N-tert-butoxycarbonyl-2-naphthylalanine cyanomethyl ester
  参考文献：
  名称：

  Methods of modifying N-termini of a peptide or protein using transferases

  摘要：

  该发明涉及使用氨酰基tRNA转移酶选择性地修改蛋白质的N-末端的方法。在某些实施例中，该方法包括将蛋白质或肽溶液与转移酶和分子衍生物接触，从而使蛋白质或肽的N-末端与该分子衍生物发生衍生化反应。

  公开号：

  US09376700B2

文献信息

• Methods of modifying N-termini of a peptide or protein using transferases
  申请人：The Trustees of the University of Pennsylvania

  公开号：US09376700B2

  公开（公告）日：2016-06-28

  The invention includes a selective method of modifying the N-terminus of a protein using an aminoacyl tRNA transferase. In certain embodiments, the method comprises contacting a solution of the protein or peptide with a transferase and a derivative of a molecule, whereby the N-terminus of the protein or peptide is derivatized with the molecule.

  该发明涉及使用氨酰基tRNA转移酶选择性地修改蛋白质的N-末端的方法。在某些实施例中，该方法包括将蛋白质或肽溶液与转移酶和分子衍生物接触，从而使蛋白质或肽的N-末端与该分子衍生物发生衍生化反应。
• ONE STEP N-TERMINAL TAGGING OF PROTEINS
  申请人：The Trustees of the University of Pennsylvania

  公开号：US20150140605A1

  公开（公告）日：2015-05-21

  The invention includes a selective method of modifying the N-terminus of a protein using an aminoacyl tRNA transferase. In certain embodiments, the method comprises contacting a solution of the protein or peptide with a transferase and a derivative of a molecule, whereby the N-terminus of the protein or peptide is derivatized with the molecule.

  本发明涉及使用氨酰tRNA转移酶选择性地改变蛋白质的N-末端的方法。在某些实施例中，该方法包括将蛋白质或肽的溶液与转移酶和分子的衍生物接触，从而使蛋白质或肽的N-末端与该分子发生衍生化反应。
• Unexpected Preference of the <i>E. coli</i> Translation System for the Ester Bond during Incorporation of Backbone-Elongated Substrates
  作者：Shinsuke Sando、Kenji Abe、Nobuhiko Sato、Toshihiro Shibata、Keigo Mizusawa、Yasuhiro Aoyama

  DOI：10.1021/ja068033n

  日期：2007.5.1

  There have been recent advances in the ribosomal synthesis of various molecules composed of nonnatural ribosomal substrates. However, the ribosome has strict limitations on substrates with elongated backbones. Here, we show an unexpected loophole in the E. coli translation system, based on a remarkable disparity in its selectivity for beta-amino/hydroxy acids. We challenged beta-hydroxypropionic acid (beta-HPA), which is less nucleophilic than beta-amino acids but free from protonation, to produce a new repertoire of ribosome-compatible but main-chain-elongated substrates. PAGE analysis and mass-coupled S-tag assays of amber suppression experiments using yeast suppressor tRNA(CUA)(Phe) confirmed the actual incorporation of beta-HPA into proteins/oligopeptides. We investigated the side-chain effects of beta-HPA and found that the side chain at position alpha and R stereochemistry of the beta-substrate is preferred and even notably enhances the efficiency of incorporation as compared to the parent substrate. These results indicate that the E. coli translation machinery can utilize main-chain-elongated substrates if the pK(a) of the substrate is appropriately chosen.
• US9376700B2
  申请人：——

  公开号：US9376700B2

  公开（公告）日：2016-06-28
• N-Terminal Protein Modification Using Simple Aminoacyl Transferase Substrates
  作者：Anne M. Wagner、Mark W. Fegley、John B. Warner、Christina L. J. Grindley、Nicholas P. Marotta、E. James Petersson

  DOI：10.1021/ja2055098

  日期：2011.9.28

  Methods for synthetically manipulating protein structure enable greater flexibility in the study of protein function. Previous characterization of the Escherichia coli aminoacyl tRNA transferase (AaT) has shown that it can modify the N-terminus of a protein with an amino acid from a tRNA or a synthetic oligonucleotide donor. Here, we demonstrate that AaT can efficiently use a minimal adenosine substrate, which can be synthesized in one to two steps from readily available starting materials. We have characterized the enzymatic activity of AaT with aminoacyl adenosyl donors and found that reaction products do not inhibit AaT. The use of adenosyl donors removes the substrate limitations imposed by the use of synthetases for tRNA charging and avoids the complex synthesis of an oligonucleotide donor. Thus, our AaT donors increase the potential substrate scope and reaction scale for N-terminal protein modification under conditions that maintain folding.