substance P | 71977-09-8

• 物质功能分类: 生物化工 - 生化试剂 - 激动剂抑制剂
• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: substance P
• 英文别名: RPKPQQFFGLM；Substance P, Free Acid；(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-5-amino-2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-1-[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-5-oxopentanoyl]amino]-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]-4-methylpentanoyl]amino]-4-methylsulfanylbutanoic acid
• CAS: 71977-09-8
• 化学式: C₆₃H₉₇N₁₇O₁₄S
• 分子量: 1348.63
• InChiKey: XHWDVRRNQHMAPE-CUZNLEPHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.9
• 重原子数：
  95
• 可旋转键数：
  42
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.59
• 拓扑面积：
  539
• 氢给体数：
  15
• 氢受体数：
  18

安全信息

• WGK Germany：
  3

制备方法与用途

生物活性

Substance P, Free Acid 是 substance P 的类似物，但不具备 substance P 的生物活性。

反应信息

• 作为反应物：
  描述：

  substance P 、 邻氨基对甲苯酚 在 potassium hexacyanoferrate(III) 作用下， 以 aq. phosphate buffer 、 乙腈 为溶剂， 反应 0.5h， 生成
  参考文献：
  名称：

  N-Terminal Modification of Proteins with o-Aminophenols

  摘要：

  The synthetic modification of proteins plays an important role in chemical biology and biomaterials science. These fields provide a constant need for chemical tools that can introduce new functionality in specific locations on protein surfaces. In this work, an oxidative strategy is demonstrated for the efficient modification of N-terminal residues on peptides and N-terminal proline residues on proteins. The strategy uses o-aminophenols or o-catechols that are oxidized to active coupling species in situ using potassium ferricyanide. Peptide screening results have revealed that many N-terminal amino acids can participate in this reaction, and that proline residues are particularly reactive. When applied to protein substrates, the reaction shows a stronger requirement for the proline group. Key advantages of the reaction include its fast second-order kinetics and ability to achieve site-selective modification in a single step using low concentrations of reagent. Although free cysteines are also modified by the coupling reaction, they can be protected through disulfide formation and then liberated after N-terminal coupling is complete. This allows access to doubly functionalized bioconjugates that can be difficult to access using other methods.

  DOI：

  10.1021/ja500728c
• 作为产物：
  描述：

  BOC-甘氨酸 、 BOC-L-亮氨酸 、 Boc-L-蛋氨酸 、 BOC-L-苯丙氨酸 、 alkaline earth salt of/the/ methylsulfuric acid 生成 substance P
  参考文献：
  名称：

  Synthesis of peptides by the solid-phase method. 7. Substance P and analogs

  摘要：

  Substance P and 21 related peptides containing isosteric or isofunctional groups were prepared by the solid-phase method. After purification by gel filtration and ion-exchange chromatography, the compounds were characterized by thin-layer chromatography, paper electrophoresis, and amino acid and elemental analysis. The biological activities of the peptides were evaluated in vitro on the guinea pig ileum, the rabbit mesenteric vein, and the dog common carotid artery and in vivo on the rat blood pressure. It is shown that the replacement of some residues in the undecapeptide substance P causes variable losses of apparent affinity with a little or no change in the intrinsic activity. All the analogues used in the present study were found to be inactive as antagonists.

  DOI：

  10.1021/jm00343a012

文献信息

• Structure and Biosynthesis of Isatropolones, Bioactive Amine-Scavenging Fluorescent Natural Products from <i>Streptomyces</i>  Gö66
  作者：Xiaofeng Cai、Yi-Ming Shi、Nicole Pöhlmann、Ole Revermann、Isabel Bahner、Sacha J. Pidot、Frank Wesche、Helmut Lackner、Claudia Büchel、Marcel Kaiser、Christian Richter、Harald Schwalbe、Timothy P. Stinear、Axel Zeeck、Helge B. Bode

  DOI：10.1002/anie.201701223

  日期：2017.4.24

  The natural products isatropolone A–C (1–3) were reisolated from Streptomyces Gö66, with 1 and 3 showing potent activity against Leishmania donovani. They contain a rare tropolone ring derived from a type II polyketide biosynthesis pathway. Their biosynthesis was elucidated by labeling experiments, analysis of the biosynthesis gene cluster, its partial heterologous expression, and structural characterization

  天然产物isatropolone A-C（1 - 3）是从再分离链霉菌Gö66，用1和3显示出对利什曼原虫的有效活性。它们含有源自II型聚酮化合物生物合成途径的稀有托酚酮环。通过标记实验，生物合成基因簇的分析，其部分异源表达以及各种中间体的结构表征，阐明了它们的生物合成。由于具有1,5-二酮部分，它们可以与氨，胺，赖氨酸和含赖氨酸的肽和蛋白质反应，从而形成共价键并随后形成吡啶环。它们的荧光性质会随着胺的结合而变化，从而使可视化的胺（包括蛋白质）简单可视化。
• Negative-Ion Electron Capture Dissociation: Radical-Driven Fragmentation of Charge-Increased Gaseous Peptide Anions
  作者：Hyun Ju Yoo、Ning Wang、Shuyi Zhuang、Hangtian Song、Kristina Håkansson

  DOI：10.1021/ja207736y

  日期：2011.10.26

  The generation of gaseous polyanions with a Coulomb barrier has attracted attention as exemplified by previous studies of fullerene dianions. However, this phenomenon has not been reported for biological anions. By contrast, electron attachment to multiply charged peptide and protein cations has seen a surge of interest due to the high utility for tandem mass spectrometry (MS/MS). Electron capture dissociation (ECD) and electron transfer dissociation (ETD) involve radical-driven fragmentation of charge-reduced peptide/protein cations to yield N-C-alpha backbone bond cleavage, resulting in predictable c'/Z(center dot)-type product ions without loss of labile post-translational modifications (PTMs). However, acidic peptides, e.g., with biologically important PTMs such as phosphorylation and sulfonation, are difficult to multiply charge in positive ion mode and show improved ionization in negative-ion mode. We found that peptide anions ([M - nH](n-), n >= 1) can capture electrons within a rather narrow energy range (similar to 3.5-6.5 eV), resulting in charge-increased radical intermediates that undergo dissociation analogous to that in ECD/ETD. Gas-phase zwitterionic structures appear to play an important role in this novel MS/MS technique, negative-ion electron capture dissociation (niECD).
• Synthesis of peptides by the solid-phase method. 7. Substance P and analogs
  作者：A. Fournier、R. Couture、D. Regoli、M. Gendreau、S. St-Pierre

  DOI：10.1021/jm00343a012

  日期：1982.1

  Substance P and 21 related peptides containing isosteric or isofunctional groups were prepared by the solid-phase method. After purification by gel filtration and ion-exchange chromatography, the compounds were characterized by thin-layer chromatography, paper electrophoresis, and amino acid and elemental analysis. The biological activities of the peptides were evaluated in vitro on the guinea pig ileum, the rabbit mesenteric vein, and the dog common carotid artery and in vivo on the rat blood pressure. It is shown that the replacement of some residues in the undecapeptide substance P causes variable losses of apparent affinity with a little or no change in the intrinsic activity. All the analogues used in the present study were found to be inactive as antagonists.
• N-Terminal Modification of Proteins with <i>o</i>-Aminophenols
  作者：Allie C. Obermeyer、John B. Jarman、Matthew B. Francis

  DOI：10.1021/ja500728c

  日期：2014.7.9

  The synthetic modification of proteins plays an important role in chemical biology and biomaterials science. These fields provide a constant need for chemical tools that can introduce new functionality in specific locations on protein surfaces. In this work, an oxidative strategy is demonstrated for the efficient modification of N-terminal residues on peptides and N-terminal proline residues on proteins. The strategy uses o-aminophenols or o-catechols that are oxidized to active coupling species in situ using potassium ferricyanide. Peptide screening results have revealed that many N-terminal amino acids can participate in this reaction, and that proline residues are particularly reactive. When applied to protein substrates, the reaction shows a stronger requirement for the proline group. Key advantages of the reaction include its fast second-order kinetics and ability to achieve site-selective modification in a single step using low concentrations of reagent. Although free cysteines are also modified by the coupling reaction, they can be protected through disulfide formation and then liberated after N-terminal coupling is complete. This allows access to doubly functionalized bioconjugates that can be difficult to access using other methods.