15N-ε-Fmoc-Lys(Boc)-OH | 934239-43-7

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: 15N-ε-Fmoc-Lys(Boc)-OH
• CAS: 934239-43-7
• 化学式: C₂₆H₃₂N₂O₆
• 分子量: 469.543
• InChiKey: UMRUUWFGLGNQLI-ZKMGEMCJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.67
• 重原子数：
  34.0
• 可旋转键数：
  9.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.42
• 拓扑面积：
  113.96
• 氢给体数：
  3.0
• 氢受体数：
  5.0

反应信息

• 作为产物：
  描述：

  、 9-芴甲基-N-琥珀酰亚胺基碳酸酯 在 三乙胺 作用下， 以 水 、 乙腈 为溶剂， 反应 0.5h， 以94%的产率得到15N-ε-Fmoc-Lys(Boc)-OH
  参考文献：
  名称：

  Functional and Mechanistic Analyses of Biomimetic Aminoacyl Transfer Reactions in de Novo Designed Coiled Coil Peptides via Rational Active Site Engineering

  摘要：

  Ribosomes and nonribosomal peptide synthetases (NRPSs) carry out instructed peptide synthesis through a series of directed intermodular aminoacyl transfer reactions. We recently reported the design of coiled-coil assemblies that could functionally mimic the elementary aminoacyl loading and intermodular aminoacyl transfer steps of NRPSs. These peptides were designed initially to accelerate aminoacyl transfer mainly through catalysis by approximation by closely juxtaposing four active site moieties, two each from adjacent noncovalently associated helical modules. In our designs peptide self-assembly positions a cysteine residue that is used to covalently capture substrates from solution via transthiolesterification (substrate loading step to generate the aminoacyl donor site) adjacent to an aminoacyl acceptor site provided by a covalently tethered amino acid or modeled by the epsilon-amine of an active site lysine. However, through systematic functional analyses of 48 rationally designed peptide sequences, we have now determined that the substrate loading and intermodular aminoacyl transfer steps can be significantly influenced (up to similar to 10(3)-fold) by engineering changes in the active site microenvironment through amino acid substitutions and variations in the inter-residue distances and geometry. Mechanistic studies based on N-15 NMR and kinetic analysis further indicate that certain active site constellations furnish an unexpectedly large pK(a) depression (1.5 pH units) of the aminoacyl-acceptor moiety, helping to explain the observed high rates of aminoacyl transfer in those constructs. Taken together, our studies demonstrate the feasibility of engineering efficient de novo peptide sequences possessing active sites and functions reminiscent of those in natural enzymes.

  DOI：

  10.1021/ja068052x