GFEIDKVWYDLDA | 1268467-89-5

• 分子结构分类: 有机化合物 - 有机聚合物 - 多肽
• 英文名称: GFEIDKVWYDLDA
• CAS: 1268467-89-5
• 化学式: C₇₄H₁₀₃N₁₅O₂₃
• 分子量: 1570.72
• InChiKey: BECASDILPBTPKS-AJBNFEDGSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.05
• 重原子数：
  112.0
• 可旋转键数：
  49.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  623.76
• 氢给体数：
  21.0
• 氢受体数：
  20.0

反应信息

• 作为反应物：
  描述：

  GFEIDKVWYDLDA 、 R-(+)-硫辛酸 在 mutant lipoic acid ligase A from Escherichia coli 作用下， 反应 0.75h， 生成
  参考文献：
  名称：

  硫辛酸连接酶与降冰片烯底物及随后的反电子需量狄尔斯-阿尔德反应的两步蛋白质标记

  摘要：

  在活细胞上标记表面蛋白：首先使用硫辛酸连接酶A的突变体将降冰片烯手柄与信号肽融合。在第二步中，将降冰片烯进行反电子需求的Diels-Alder环加成反应，并用四嗪修饰的四甲基罗丹明部分。降冰片烯手柄在活细胞条件下具有很高的稳定性，并且易于合成。

  DOI：

  10.1002/cbic.201500042

文献信息

• Synthesis of 7-Aminocoumarin by Buchwald-Hartwig Cross Coupling for Specific Protein Labeling in Living Cells
  作者：Xin Jin、Chayasith Uttamapinant、Alice Y. Ting

  DOI：10.1002/cbic.201000414

  日期：2011.1.3

  PRIME time: We report the synthesis of a pH‐insensitive blue fluorophore, 7‐aminocoumarin, by using palladium‐ catalyzed Buchwald–Hartwig cross coupling. 7‐Aminocoumarin can be used to tag recombinant proteins on the cell surface and inside living cells through PRIME (probe incorporation mediated by enzymes), and unlike 7‐hydroxycoumarin, can be visualized in acidic organelles such as endosomes.

  PRIME 时间：我们报告了使用钯催化的 Buchwald-Hartwig 交叉偶联合成 pH 不敏感的蓝色荧光团 7-氨基香豆素。7-氨基香豆素可用于通过 PRIME（酶介导的探针掺入）标记细胞表面和活细胞内部的重组蛋白，并且与 7-羟基香豆素不同，可以在酸性细胞器（如内体）中观察。
• Computational design of a red fluorophore ligase for site-specific protein labeling in living cells
  作者：Daniel S. Liu、Lucas G. Nivón、Florian Richter、Peter J. Goldman、Thomas J. Deerinck、Jennifer Z. Yao、Douglas Richardson、William S. Phipps、Anne Z. Ye、Mark H. Ellisman、Catherine L. Drennan、David Baker、Alice Y. Ting

  DOI：10.1073/pnas.1404736111

  日期：2014.10.28

  This work establishes a fluorescence labeling method that can be used in living cells to derivatize specific proteins of interest with a small red fluorophore, resorufin. The method has extremely high sequence specificity and is based on a computationally designed fluorophore ligase, derived from Escherichia coli lipoic acid ligase. These results demonstrate the power of computational design to majorly reengineer enzyme specificity. Extensive screening of rationally designed enzyme mutants failed to achieve the same result.

  这项工作建立了一种荧光标记方法，可在活细胞中使用，用小红色荧光素resorufin对感兴趣的特定蛋白进行衍生化。该方法具有极高的序列特异性，基于计算设计的荧光素连接酶，源自大肠杆菌硫辛酸连接酶。这些结果展示了计算设计在重塑酶特异性方面的强大能力。对经过合理设计的酶突变体进行广泛筛选未能达到相同结果。
• Two-Step Protein Labeling Utilizing Lipoic Acid Ligase and Sonogashira Cross-Coupling
  作者：Sebastian Hauke、Marcel Best、Tobias T. Schmidt、Mathis Baalmann、André Krause、Richard Wombacher

  DOI：10.1021/bc500349h

  日期：2014.9.17

  Labeling proteins in their natural settings with fluorescent proteins or protein tags often leads to problems. Despite the high specificity, these methods influence the natural functions due to the rather large size of the proteins used. Here we present a two-step labeling procedure for the attachment of various fluorescent probes to a small peptide sequence (13 amino acids) using enzyme-mediated peptide

  用荧光蛋白或蛋白标签在其自然环境中标记蛋白经常会导致问题。尽管具有很高的特异性，但由于所用蛋白质的尺寸较大，这些方法仍会影响自然功能。在这里，我们提出了一个两步的标记程序，使用酶介导的肽标记结合钯催化的Sonogashira交叉偶联，将各种荧光探针连接到一个小的肽序列（13个氨基酸）。我们从一个小文库中鉴定了对碘苯衍生物，该文库可以通过大肠杆菌硫辛酸连接酶A（LplA）共价连接至特定13个氨基酸肽序列中的赖氨酸残基。p的衍生碘代苯基随后在肽以及蛋白质水平上用作生物正交过渡金属催化的Sonogashira交叉偶联与炔基官能化的荧光团的偶联。我们的两步标记策略将酶介导标记的高选择性与钯催化的Sonogashira交叉偶联的化学选择性结合在一起。
• Location-agnostic site-specific protein bioconjugation via Baylis Hillman adducts
  作者：Mudassir H. Mir、Sangeeta Parmar、Chhaya Singh、Dimpy Kalia

  DOI：10.1038/s41467-024-45124-2

  日期：——

  Proteins labelled site-specifically with small molecules are valuable assets for chemical biology and drug development. The unique reactivity profile of the 1,2-aminothiol moiety of N-terminal cysteines (N-Cys) of proteins renders it highly attractive for regioselective protein labelling. Herein, we report an ultrafast Z-selective reaction between isatin-derived Baylis Hillman adducts and 1,2-aminothiols to form a bis-heterocyclic scaffold, and employ it for stable protein bioconjugation under both in vitro and live-cell conditions. We refer to our protein bioconjugation technology as Baylis Hillman orchestrated protein aminothiol labelling (BHoPAL). Furthermore, we report a lipoic acid ligase-based technology for introducing the 1,2-aminothiol moiety at any desired site within proteins, rendering BHoPAL location-agnostic (not limited to N-Cys). By using this approach in tandem with BHoPAL, we generate dually labelled protein bioconjugates appended with different labels at two distinct specific sites on a single protein molecule. Taken together, the protein bioconjugation toolkit that we disclose herein will contribute towards the generation of both mono and multi-labelled protein-small molecule bioconjugates for applications as diverse as biophysical assays, cellular imaging, and the production of therapeutic protein–drug conjugates. In addition to protein bioconjugation, the bis-heterocyclic scaffold we report herein will find applications in synthetic and medicinal chemistry.