Fmoc-Dab(Mtt)-OH

• 分子结构分类: 有机化合物 - 苯类化合物 - 三苯基化合物
• 英文名称: Fmoc-Dab(Mtt)-OH
• 英文别名: (2S)-2-(9H-fluoren-9-ylmethoxycarbonylamino)-4-[[(4-methylphenyl)-diphenylmethyl]amino]butanoic acid
• 化学式: C₃₉H₃₆N₂O₄
• 分子量: 596.726
• InChiKey: RXKBBKLPMHPIKD-BHVANESWSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  5.4
• 重原子数：
  45
• 可旋转键数：
  12
• 环数：
  6.0
• sp3杂化的碳原子比例：
  0.18
• 拓扑面积：
  87.7
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  Fmoc-Dab(Mtt)-OH 、 Fmoc-O-叔丁基-L-谷氨酸 、 Fmoc-L-异亮氨酸 、 dapoxylsulfonyl chloride 生成 (4S)-4-acetamido-5-[[(2S)-1-[[(2S)-1-[[(2S,3S)-1-[[(2S)-1-[[2-[[(2S)-1-[[(2S,3S)-1-[[(2S)-1-[[(2S)-1-amino-1-oxopropan-2-yl]amino]-4-[[4-[5-[4-(dimethylamino)phenyl]-1,3-oxazol-2-yl]phenyl]sulfonylamino]-1-oxobutan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-2-oxoethyl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-4-carboxy-1-oxobutan-2-yl]amino]-5-oxopentanoic acid
  参考文献：
  名称：

  Phosphorylation-Driven Protein−Protein Interactions:  A Protein Kinase Sensing System

  摘要：

  A highly flexible protein kinase sensing system is described that furnishes severalfold changes in fluorescence in response to phosphorylation. A library of Src kinase peptide substrates was prepared that contained different environmentally sensitive fluorophores positioned at various sites on the active site directed sequence. Robust changes in fluorescent intensity were observed in the presence of a phosphotyrosine binding domain protein (Lck SH2 domain), which furnishes a hydrophobic environment for the fluorophore. This protein kinase sensing system has the advantages that the fluorescent indicator can be unobtrusively positioned on the peptide substrate, and that different environmentally sensitive fluorophores with distinct photophysical properties can be employed.

  DOI：

  10.1021/ja050789j

文献信息

• Macrocyclic Modalities Combining Peptide Epitopes and Natural Product Fragments
  作者：Stéphanie M. Guéret、Sasikala Thavam、Rodrigo J. Carbajo、Marco Potowski、Niklas Larsson、Göran Dahl、Anita Dellsén、Tom N. Grossmann、Alleyn T. Plowright、Eric Valeur、Malin Lemurell、Herbert Waldmann

  DOI：10.1021/jacs.0c00269

  日期：2020.3.11

  loop” protein segments have variable structure and conformation and contribute crucially to protein–protein interactions. We describe a new hot loop mimicking modality, termed PepNats, in which natural product (NP)-inspired structures are incorporated as conformation-determining and -restricting structural elements into macrocyclic hot loop-derived peptides. Macrocyclic PepNats representing hot loops of

  “热环”蛋白质片段具有可变的结构和构象，对蛋白质-蛋白质相互作用至关重要。我们描述了一种新的热循环模拟模式，称为 PepNats，其中天然产物 (NP) 启发的结构作为构象决定和限制结构元素被纳入大环热循环衍生肽中。代表诱导型一氧化氮合酶 (iNOS) 和人类刺鼠相关蛋白 (AGRP) 热循环的大环 PepNats 在固体支持物上合成，采用亚胺形成的大环化和随后的立体选择性 1,3-偶极环加成作为关键步骤。源自 iNOS DINNN 热环和 AGRP RFF 热点序列的 PepNats 产生了与 iNOS 结合的含有 SPRY 结构域的 SOCS 盒蛋白 2 (SPSB2) 的新型有效配体，和 AGRP 结合黑皮质素 (MC) 受体的选择性配体。NP 启发的片段绝对构型决定了负责结合的肽部分的构象。这些结果表明，NP 启发的支架与肽表位的组合能够鉴定具有构象受限和生物相关结构的新型热环模拟物。
• Photo-induced crosslinking uncovers an antiparallel strand orientation in heterodimeric (EIAALEK)₃/(KIAALKE)₃and (EIAALEK)₃/(RIAALRE)₃coiled-coil systems
  作者：D. Aerssens、L. Miret-Casals、D. Gomez、D. Sousa-Neves、Y. Levy、M. De Vleesschouwer、A. Manicardi、A. Madder

  DOI：10.1039/d2ob02181a

  日期：——

  Experimental and computational support is provided for co-existence of parallel and antiparallel conformations of the E3/K3 and E3/R3 coiled-coil systems in solution.

  实验和计算支持了 E3/K3 和 E3/R3 螺旋线圈系统在溶液中平行和反平行构象的共存。
• Phosphorylation-Driven Protein−Protein Interactions:  A Protein Kinase Sensing System
  作者：Qunzhao Wang、David S. Lawrence

  DOI：10.1021/ja050789j

  日期：2005.6.1

  A highly flexible protein kinase sensing system is described that furnishes severalfold changes in fluorescence in response to phosphorylation. A library of Src kinase peptide substrates was prepared that contained different environmentally sensitive fluorophores positioned at various sites on the active site directed sequence. Robust changes in fluorescent intensity were observed in the presence of a phosphotyrosine binding domain protein (Lck SH2 domain), which furnishes a hydrophobic environment for the fluorophore. This protein kinase sensing system has the advantages that the fluorescent indicator can be unobtrusively positioned on the peptide substrate, and that different environmentally sensitive fluorophores with distinct photophysical properties can be employed.