N-succinimidyl-N'-biotinyl-3,6-dioxaoctane-1,8-diamine | 138529-52-9

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 生物素及其衍生物
• 英文名称: N-succinimidyl-N'-biotinyl-3,6-dioxaoctane-1,8-diamine
• 英文别名: 4-[2-[2-[2-[5-[(3aS,4S,6aR)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoylamino]ethoxy]ethoxy]ethylamino]-4-oxobutanoic acid
• CAS: 138529-52-9
• 化学式: C₂₀H₃₄N₄O₇S
• 分子量: 474.579
• InChiKey: SGTQZPPEZURAFU-DOXZYTNZSA-N

物化性质

• 沸点：
  878.0±65.0 °C(Predicted)
• 密度：
  1.241±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.5
• 重原子数：
  32
• 可旋转键数：
  17
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.8
• 拓扑面积：
  180
• 氢给体数：
  5
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  N-succinimidyl-N'-biotinyl-3,6-dioxaoctane-1,8-diamine 在 4-二甲氨基吡啶 、 三正丁胺 、 N,N-二异丙基乙胺 、 N-[(dimethylamino)-3-oxo-1H-1,2,3-triazolo[4,5-b]pyridin-1-yl-methylene]-N-methylmethanaminium hexafluorophosphate 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 反应 5.0h， 生成
  参考文献：
  名称：

  A Modular Cross-Linking Approach for Exploring Protein Interactions

  摘要：

  A method is described for the elucidation of protein-protein interactions using novel cross-linking reagents and mass spectrometry. The method incorporates (1) a modular solid-phase synthetic strategy for generating the cross-linking reagents, (2) enrichment and digestion of cross-linked proteins using microconcentrators, (3) mass spectrometric analysis of cross-linked peptides, and (4) comprehensive computational analysis of the cross-linking data. This integrated approach has been applied to the study of cross-linking between the components of the heterodimeric protein complex negative cofactor 2.

  DOI：

  10.1021/ja026917a
• 作为产物：
  描述：

  N-Boc-N'-biotinyl-3,6-dioxaoctane-1,8-diamine 在 苯甲醚 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 乙腈 为溶剂， 反应 2.0h， 生成 N-succinimidyl-N'-biotinyl-3,6-dioxaoctane-1,8-diamine
  参考文献：
  名称：

  A Modular Cross-Linking Approach for Exploring Protein Interactions

  摘要：

  A method is described for the elucidation of protein-protein interactions using novel cross-linking reagents and mass spectrometry. The method incorporates (1) a modular solid-phase synthetic strategy for generating the cross-linking reagents, (2) enrichment and digestion of cross-linked proteins using microconcentrators, (3) mass spectrometric analysis of cross-linked peptides, and (4) comprehensive computational analysis of the cross-linking data. This integrated approach has been applied to the study of cross-linking between the components of the heterodimeric protein complex negative cofactor 2.

  DOI：

  10.1021/ja026917a

文献信息

• Fast and Stable N‐Terminal Cysteine Modification through Thiazolidino Boronate Mediated Acyl Transfer
  作者：Kaicheng Li、Wenjian Wang、Jianmin Gao

  DOI：10.1002/anie.202000837

  日期：2020.8.17

  facile modification of NCys‐bearing proteins in complex biological milieu. This new NCys conjugation proceeds via a thiazolidine boronate (TzB) intermediate that results from fast (k 2: ≈5000 m −1 s−1) and reversible conjugation of NCys with 2‐formylphenylboronic acid (FPBA). We designed a FPBA derivative that upon TzB formation elicits intramolecular acyl transfer to give N‐acyl thiazolidines. In contrast

  我们报告了一种 N 端半胱氨酸 (NCys) 的新型偶联物，该偶联物具有快速动力学和精细的选择性，从而能够在复杂的生物环境中轻松修饰携带 NCys 的蛋白质。这种新的 NCys 共轭通过噻唑烷硼酸酯 (TzB) 中间体进行，该中间体由快速 ( k 2 : ≈5000  m -1  s -1) 和 NCys 与 2-甲酰基苯基硼酸 (FPBA) 的可逆共轭。我们设计了一种 FPBA 衍生物，它在 TzB 形成时引发分子内酰基转移，得到 N-酰基噻唑烷。与 TzB 的快速水解相反，N-酰化噻唑烷在生理条件下表现出强大的稳定性。TzB 介导的 NCys 偶联的效用通过两种酶的快速和非破坏性标记来证明。此外，将这种化学应用于噬菌体可以轻松地对噬菌体库进行化学修饰，这大大扩展了适合噬菌体展示的化学空间。
• Design, Synthesis, and Application of a Hydrazide-Functionalized Isotope-Coded Affinity Tag for the Quantification of Oxylipid−Protein Conjugates
  作者：Bingnan Han、Jan F. Stevens、Claudia S. Maier

  DOI：10.1021/ac062262a

  日期：2007.5.1

  An isotopically coded affinity probe was developed and evaluated for the characterization and quantification of proteins adducted by 2-alkenals derived from lipid peroxidation (LPO) processes. Lipid-derived 2-alkenals, such as acrolein and 4-hydroxy-2-nonenal (HNE), have the ability to react with cysteine, histidine, and lysine residues in proteins, thus causing protein damage and loss of protein function. Such modifications of proteins are difficult to characterize in biological samples by mass spectrometry due to the complexity of protein extracts and the low abundance of adducted proteins. The novel aldehyde-reactive, hydrazide-functionalized, isotope-coded affinity tag (HICAT) described in this study was found effective for the selective isolation, detection, and quantification of Michael-type adducts of 2-alkenals with proteins using a combination of affinity isolation, nanoLC, and matrix-assisted laser desorption ionization tandem mass spectrometry (MALDI-MS/MS). The chemical and mass spectrometric properties of the new probe are demonstrated on a model protein treated with HNE. The efficacy of HICAT for the analysis of complex samples was tested using preparations of mitochondrial proteins that were modified in vitro with HNE. The potential of the HICAT strategy for the identification, characterization, and quantification of in vivo oxylipid−protein conjugates is demonstrated on cardiac mitochondrial protein preparations, in which, for example, the ADP/ATP translocase 1 was found adducted to the 2-alkenals, acrolein and 4-hydroxy-2-hexenal, at Cys-256.

  开发并评估了一种同位素编码的亲和探针，用于表征和量化被脂质过氧化（LPO）过程中产生的 2-烯烃吸附的蛋白质。脂质衍生的 2-烯烃（如丙烯醛和 4-羟基-2-壬烯醛 (HNE)）能够与蛋白质中的半胱氨酸、组氨酸和赖氨酸残基发生反应，从而导致蛋白质损伤和蛋白质功能丧失。由于蛋白质提取物的复杂性和加合物蛋白质的低丰度，很难通过质谱法表征生物样本中蛋白质的这种修饰。本研究中描述的新型醛反应、酰肼功能化、同位素编码的亲和标签（HICAT）可通过亲和分离、纳米液相色谱法和基质辅助激光解吸电离串联质谱法（MALDI-MS/MS）有效地选择性分离、检测和定量 2-烯烃与蛋白质的迈克尔型加合物。新探针的化学和质谱特性在一种经 HNE 处理的模型蛋白质上得到了验证。使用经 HNE 体外修饰的线粒体蛋白质制备物测试了 HICAT 分析复杂样品的功效。在心脏线粒体蛋白质制备物上证明了 HICAT 策略在鉴定、表征和定量体内氧化脂质-蛋白质共轭物方面的潜力，例如，在其中发现 ADP/ATP 转位酶 1 在 Cys-256 处与 2-烯烃、丙烯醛和 4-羟基-2-己烯醛加成。
• ANTI-MUC1 ANTIBODY
  申请人：Shionogi & Co., Ltd.

  公开号：EP2351777B1

  公开（公告）日：2015-10-28
• An Apoptosis‐Inducing Small Molecule That Binds to Heat Shock Protein 70
  作者：Darren R. Williams、Sung‐Kyun Ko、Sungjin Park、Myung‐Ryul Lee、Injae Shin

  DOI：10.1002/anie.200802801

  日期：2008.9.15
• A Modular Cross-Linking Approach for Exploring Protein Interactions
  作者：Michelle Trester-Zedlitz、Katsuhiko Kamada、Stephen K. Burley、David Fenyö、Brian T. Chait、Tom W. Muir

  DOI：10.1021/ja026917a

  日期：2003.3.1

  A method is described for the elucidation of protein-protein interactions using novel cross-linking reagents and mass spectrometry. The method incorporates (1) a modular solid-phase synthetic strategy for generating the cross-linking reagents, (2) enrichment and digestion of cross-linked proteins using microconcentrators, (3) mass spectrometric analysis of cross-linked peptides, and (4) comprehensive computational analysis of the cross-linking data. This integrated approach has been applied to the study of cross-linking between the components of the heterodimeric protein complex negative cofactor 2.