Boc-AU-OBzl | 79118-33-5

• 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: Boc-AU-OBzl
• 英文别名: Boc-Ala-Aib-OBzl；BocAlaAibOBn
• CAS: 79118-33-5
• 化学式: C₁₉H₂₈N₂O₅
• 分子量: 364.442
• InChiKey: AQHLXVKDLMYTGA-ZDUSSCGKSA-N

物化性质

• 沸点：
  516.5±35.0 °C(Predicted)
• 密度：
  1.117±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.54
• 重原子数：
  26.0
• 可旋转键数：
  6.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  93.73
• 氢给体数：
  2.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  Boc-AU-OBzl 在 palladium on activated charcoal N-甲基吗啉 、 氢气 、 1-羟基苯并三唑 、 1-(3-二甲基氨基丙基)-3-乙基碳二亚胺 作用下， 以 乙醇 、 N,N-二甲基甲酰胺 为溶剂， 25.0 ℃ 、101.33 kPa 条件下， 反应 36.0h， 生成 2-{(S)-2-[2-((S)-2-tert-Butoxycarbonylamino-propionylamino)-2-methyl-propionylamino]-propionylamino}-2-methyl-propionic acid benzyl ester
  参考文献：
  名称：

  Joshi, Hemant V.; Meier, Mark S., Journal of the American Chemical Society, 1996, vol. 118, # 48, p. 12038 - 12044

  摘要：

  DOI：
• 作为产物：
  描述：

  N-叔丁氧羰基-L-丙氨酸 在 N-甲基吗啉 作用下， 以 四氢呋喃 为溶剂， 生成 Boc-AU-OBzl
  参考文献：
  名称：

  Joshi, Hemant V.; Meier, Mark S., Journal of the American Chemical Society, 1996, vol. 118, # 48, p. 12038 - 12044

  摘要：

  DOI：

文献信息

• Synthesis, Preferred Conformation, and Membrane Activity of Medium-Length Peptaibiotics: Tylopeptin B
  作者：Marina Gobbo、Claudia Poloni、Marta De Zotti、Cristina Peggion、Barbara Biondi、Gema Ballano、Fernando Formaggio、Claudio Toniolo

  DOI：10.1111/j.1747-0285.2009.00920.x

  日期：2010.2

  The solid‐phase synthesis and full chemical characterization of the medium‐length (14‐amino acid residues) peptaibol with antibiotic properties of tylopeptin B, originally extracted from the fruiting body of the mushroom Tylopilus neofelleus, are described. These data are accompanied by the results on the solution‐phase synthesis via the segment condensation approach of a selected, side‐chain protected

  描述了最初从蘑菇Tylopilus neofelleus的子实体中提取的具有酪胺肽B的抗生素特性的中等长度（14个氨基酸残基）肽醇的固相合成和完整化学特征。这些数据都伴随着在溶液相合成的结果通过一个选择的，侧链保护的，模拟的段缩合方法。通过结合使用FTIR吸收，圆二色性和2D-NMR（后一种技术与分子动力学计算相结合）进行的溶液构象分析，得出的结论是，酪蛋白B的3D结构在很大程度上是螺旋形的，并且优先考虑α-或3 10螺旋类型取决于溶剂的性质。螺旋拓扑和（部分）两亲性特征是这种肽生物素所观察到的膜修饰特性的原因。
• Solution Synthesis, Conformational Analysis, and Antimicrobial Activity of Three Alamethicin F50/5 Analogs Bearing a Trifluoroacetyl Label
  作者：Marta De Zotti、Gema Ballano、Micha Jost、Evgeniy S. Salnikov、Burkhard Bechinger、Simona Oancea、Marco Crisma、Claudio Toniolo、Fernando Formaggio

  DOI：10.1002/cbdv.201300394

  日期：2014.8

  We prepared, by solution‐phase methods, and fully characterized three analogs of the membrane‐active peptaibiotic alamethicin F50/5, bearing a single trifluoroacetyl (Tfa) label at the N‐terminus, at position 9 (central region) or at position 19 (C‐terminus), and with the three Gln at positions 7, 18, and 19 replaced by Glu(OMe) residues. To add the Tfa label at position 9 or 19, a γ‐trifluoroacetylated

  我们通过液相方法制备并充分表征了膜活性肽生物阿拉米霉素 F50/5 的三种类似物，在 N 端、位置 9（中心区域）或位置 19 带有单个三氟乙酰 (Tfa) 标签（C 端），并且第 7、18 和 19 位的三个 Gln 被 Glu(OMe) 残基取代。为了在第 9 或 19 位添加 Tfa 标记，加入了一个 γ-三氟乙酰化 α,γ-二氨基丁酸 (Dab) 残基作为原始 Val9 或 Glu(OMe)19 氨基酸的替代。我们对三种类似物进行了详细的构象分析（使用 FT-IR 吸收、CD、2D-NMR 和 X 射线衍射），这清楚地表明 Tfa 标记不会在主要的 α 螺旋结构中引入任何显着的骨架修饰亲本 peptaibiotic。对其中一种类似物的初步固态 19F-NMR 研究结果支持以下结论：Tfa 基团是分析肽生物膜相互作用的非常有前途的报告基因。最后，我们发现三种新合成的类似物的抗菌活性取决于
• Synthesis and characterization of the major component of alamethicin
  作者：T. M. Balasubramanian、Nancy C. E. Kendrick、Melissa Taylor、Garland R. Marshall、James E. Hall、Igor Vodyanoy、Fritz Reusser

  DOI：10.1021/ja00410a024

  日期：1981.10
• Aral, Toru; Tsukuni, Akio; Kawazu, Katsumi, Journal of the Chemical Society. Perkin transactions II, 2000, # 7, p. 1381 - 1390
  作者：Aral, Toru、Tsukuni, Akio、Kawazu, Katsumi、Aoi, Hironao、Hamada, Takahiro、Nishino, Norikazu

  DOI：——

  日期：——
• Cyclopentapeptides as Flexible Conformational Templates
  作者：Gregory V. Nikiforovich、Katalin E. Kövér、Wei-Jun Zhang、Garland R. Marshall

  DOI：10.1021/ja991728m

  日期：2000.4.1

  Studies of 3D models for cyclopentapeptides (CPP's) employing only NMR spectroscopy encounter a serious problem. Because of conformer averaging, 3D structure(s) derived directly from NMR data may not correspond to the energy minimum (minima) with low relative conformational energy. At the same time, independent energy calculations can determine all low-energy conformers For the CPP backbone. The two approaches are compared in this study by results obtained for cyclo(D-Pro(1)-Ala(2)-Ala(3)-Ala(4)-Ala(5)). Contrary to the conclusion (predominance of the beta II'gamma type conformer) of earlier NMR studies, independent energy calculations found a different family of low-energy 3D structures that are consistent both with the NMR data in DMSO and with the known X-ray data on CPP's. The preferable Ala(4) conformations were found in the alpha(R)/alpha(L) regions suggesting studies of cyclo(D-Pro(1)-Ala(2)-Ala(3)-Aib(4)-Ala(5)) which was synthesized. Further NMR studies confirmed the results of the independent energy calculations, The independent energy calculations have been applied also to cyclo(Arg(1)-Gly(2)-Asp(3)-D-Phe(4)-Val(5)) and cyclo(Arg(1)-Gly(2)-Asp(3)-Phe(4)-D-Val(5)). Both peptides are almost equally potent inhibitors of binding of alpha(IIb)beta(3) integrins to fibrinogen and of alpha v beta(3) integrins to vitronectin. If both of them possess a NMR-predicted conformer of the beta II'gamma type, however, the conformations of the active sequence, Arg(1)-Gly(2)-Asp(3), should be dissimilar in these two peptides, This discrepancy is eliminated in the 3D pharmacophore model proposed by independent energy calculations. The model is also in good agreement with the model by other authors that was confirmed by X-ray studies.