N-(tert-butyloxycarbonyl)-3-(3-acetyl-4-hydroxyphenyl)-L-alanine | 269745-72-4

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: N-(tert-butyloxycarbonyl)-3-(3-acetyl-4-hydroxyphenyl)-L-alanine
• 英文别名: 3-acetyl-N-(tert-butoxycarbonyl)-L-tyrosine；3-acetyl-N-(tertbutoxycarbonyl)-L-tyrosine；3-acetyl-N-Boc-L-tyrosine；(2S)-3-(3-acetyl-4-hydroxyphenyl)-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid
• CAS: 269745-72-4
• 化学式: C₁₆H₂₁NO₆
• 分子量: 323.346
• InChiKey: AAHFOEZAKOEYRF-LBPRGKRZSA-N

物化性质

• 熔点：
  110-112 °C
• 沸点：
  524.8±50.0 °C(Predicted)
• 密度：
  1.250±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  23
• 可旋转键数：
  7
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  113
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N-(tert-butyloxycarbonyl)-3-(3-acetyl-4-hydroxyphenyl)-L-alanine 在 盐酸 、 双氧水 、 碳酸氢钠 、 sodium hydroxide 作用下， 以 1,4-二氧六环 、 乙醇 、 水 、 乙腈 为溶剂， 反应 31.0h， 生成 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-3-[2-(2-furyl)-3-hydroxy-4-oxo-4H-chromen-6-yl]-L-alanine
  参考文献：
  名称：

  色氨酸的双色荧光l-氨基酸模拟物，用于探测肽-核酸复合物

  摘要：

  非天然氨基酸是用于肽性质和相互作用的位点选择性探测的重要工具。在此，首次合成了具有激发态分子内质子转移（ESIPT）和水合敏感性双重发射的荧光1-氨基酸。它是l的类似物-色氨酸带有稍大的2-（2-呋喃基）-3-羟基色酮芳族部分而不是吲哚。这种新氨基酸通过固相合成并入了NC（11-55），NC-1（HIV-1核衣壳蛋白的锌指结构域），具有强大的分子伴侣特性。它取代了位于远端手指基序和NC（11-55）手指之间的接头中的Trp37和Ala30残基。尽管高度保守的Trp37残基在NC（11-55）结构和活性中起关键作用，但它被新的荧光类似物取代后仍保留了肽的折叠，核酸结合和分子伴侣活性，表明该新氨基酸可以保守地替代Trp残基。在寡核苷酸存在的情况下，Trp37取代的肽而不是Ala30变体，表现出与局部脱水相对应的双重排放的强烈变化。结果与NMR数据一致，表明荧光氨基酸类似于Trp37与核碱基的相

  DOI：

  10.1021/bc300464u
• 作为产物：
  描述：

  L-酪氨酸 在 aluminum (III) chloride 、 sodium carbonate 作用下， 以 四氢呋喃 、 水 、 硝基苯 为溶剂， 反应 11.17h， 生成 N-(tert-butyloxycarbonyl)-3-(3-acetyl-4-hydroxyphenyl)-L-alanine
  参考文献：
  名称：

  Iminoboronate-Based Peptide Cyclization That Responds to pH, Oxidation, and Small Molecule Modulators

  摘要：

  As a rich source of therapeutic agents, peptide natural products usually adopt a cyclic or multicyclic scaffold that minimizes structural flexibility to favor target binding. Inspired by nature, chemists have been interested in developing synthetic cyclic and multicyclic peptides that serve as biological probes and potential therapeutics. Herein we describe a novel strategy for peptide cyclization in which intramolecular iminoboronate formation allows spontaneous cyclization under physiologic conditions to yield monocyclic and bicyclic peptides. Importantly the iminoboronate-based cyclization can be rapidly reversed in response to multiple stimuli, including pH, oxidation, and small molecules. This highly versatile strategy for peptide cyclization should find applications in many areas of chemical biology.

  DOI：

  10.1021/jacs.5b12301

文献信息

• Fluorescent Amino Acid Undergoing Excited State Intramolecular Proton Transfer for Site-Specific Probing and Imaging of Peptide Interactions
  作者：Marianna Sholokh、Oleksandr M. Zamotaiev、Ranjan Das、Viktoriia Y. Postupalenko、Ludovic Richert、Denis Dujardin、Olga A. Zaporozhets、Vasyl G. Pivovarenko、Andrey S. Klymchenko、Yves Mély

  DOI：10.1021/jp508748e

  日期：2015.2.12

  aromatic moieties. The strongest restriction and thus the longest fluorescence lifetimes were observed at position 37 in complexes with nucleic acids, where the probe likely stacks with the nucleobases. Based on the dependence of the lifetime values on the nature of the ligand and the labeled position, two-photon fluorescence lifetime imaging was used to identify the binding partners of the labeled peptides

  带有环境敏感荧光团的荧光氨基酸是用于肽/配体相互作用的位点选择性探测的极有价值的工具。在此，我们合成了荧光升-带有4'-甲氧基-3-羟基黄酮荧光团（M3HFaa）的氨基酸，由于激发态分子内质子转移（ESIPT）而显示出双重发射。与以前的类似物相比，发现M3HFaa的双重发射对水合作用更加敏感。通过替换HIV-1核衣壳肽的Ala30和Trp37残基，观察到M3HFaa保留了肽的结构和功能。标记的肽与核酸和脂质囊泡的相互作用在其双重发射中产生了强烈的转换，有利于ESIPT产物的发射。由于复合物中的刚性环境限制了M3HFaa芳香族部分的相对运动，因此该开关与ESIPT产品的荧光寿命长寿相关。在与核酸复合物中的第37位观察到了最强的限制，因此最长的荧光寿命，其中探针可能与核碱基堆积在一起。基于寿命值对配体性质和标记位置的依赖性，使用双光子荧光寿命成像来鉴定显微注射到活细胞中的标记肽的结合伴侣。因此
• Dual-Fluorescence <scp>l</scp>-Amino Acid Reports Insertion and Orientation of Melittin Peptide in Cell Membranes
  作者：Viktoriia Y. Postupalenko、Oleksandr M. Zamotaiev、Volodymyr V. Shvadchak、Aleksandr V. Strizhak、Vasyl G. Pivovarenko、Andrey S. Klymchenko、Yves Mely

  DOI：10.1021/bc400325n

  日期：2013.12.18

  Monitoring insertion and orientation of peptides in situ on cell membranes remains a challenge. To this end, we synthesized an L-amino acid (AFaa) containing a dual-fluorescence dye of the 3-hydroxyflavone family, as a side chain. In contrast to other labeling approaches using a flexible linker, the AFaa fluorophore, introduced by solid phase synthesis into desired position of a peptide, is attached closely to its backbone with well-defined orientation, and, therefore, could reflect its localization in the membrane. This concept was validated by replacing the leucine-9 (L9) and tryptophan-19 (W19) residues by AFaa in melittin, a well-studied membrane-active peptide. Due to high sensitivity of AFaa dual emission to the environment polarity, we detected a much deeper insertion of L9 peptide position into the bilayer, compared to the W19 position. Moreover, using fluorescence microscopy with a polarized light excitation, we found different orientation of AFaa at L9 and W19 positions of melittin in the bilayers of giant vesicles and cellular membranes. These results suggested that in the natural membranes, similarly to the model lipid bilayers, melittin is preferentially oriented parallel to the membrane surface. The developed amino acid and the proposed methodology will be of interest to study other membrane peptides.
• An Improved Synthesis of Selectively Protected <scp>l</scp>-Dopa Derivatives from <scp>l</scp>-Tyrosine
  作者：Chen、Yun-Fei Zhu、Keith Wilcoxen

  DOI：10.1021/jo9913661

  日期：2000.4.1
• WO2024096067A1
  申请人：——

  公开号：——

  公开（公告）日：——
• Iminoboronate-Based Peptide Cyclization That Responds to pH, Oxidation, and Small Molecule Modulators
  作者：Anupam Bandyopadhyay、Jianmin Gao

  DOI：10.1021/jacs.5b12301

  日期：2016.2.24

  As a rich source of therapeutic agents, peptide natural products usually adopt a cyclic or multicyclic scaffold that minimizes structural flexibility to favor target binding. Inspired by nature, chemists have been interested in developing synthetic cyclic and multicyclic peptides that serve as biological probes and potential therapeutics. Herein we describe a novel strategy for peptide cyclization in which intramolecular iminoboronate formation allows spontaneous cyclization under physiologic conditions to yield monocyclic and bicyclic peptides. Importantly the iminoboronate-based cyclization can be rapidly reversed in response to multiple stimuli, including pH, oxidation, and small molecules. This highly versatile strategy for peptide cyclization should find applications in many areas of chemical biology.