Boc-L-Leu-DL-(β-OH)-Phe-OH | 107694-12-2

• 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-L-Leu-DL-(β-OH)-Phe-OH
• 英文别名: Boc-L-Leu-DL-Phe(β-OH)-OH；Boc-Leu-DL-Phe(β-OH)-OH；Boc-Leu-(β-OH)-Phe-OH；Boc-Leu-(β-OH)Phe-OH；Boc-Leu-D,L-Phe(beta-OH)-OH；3-hydroxy-2-[[(2S)-4-methyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoyl]amino]-3-phenylpropanoic acid
• CAS: 107694-12-2
• 化学式: C₂₀H₃₀N₂O₆
• 分子量: 394.468
• InChiKey: DMIQXSHKHKYXKC-FHERZECASA-N

物化性质

• 沸点：
  622.6±55.0 °C(Predicted)
• 密度：
  1.185±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  28
• 可旋转键数：
  10
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.55
• 拓扑面积：
  125
• 氢给体数：
  4
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  Boc-L-Leu-DL-(β-OH)-Phe-OH 在 sodium acetate 作用下， 以 乙酸酐 、 N,N-二甲基甲酰胺 为溶剂， 反应 32.0h， 生成 Boc-L-Leu-ΔPhe-(Aib)3-OMe
  参考文献：
  名称：

  一锅光学分辨率的寡肽螺旋通过人工肽捆绑。

  摘要：

  DOI：

  10.1002/anie.200460703
• 作为产物：
  描述：

  Boc-L-Leu-DL-Phe(β-OH)-OMe 在 sodium hydroxide 作用下， 以 甲醇 为溶剂， 生成 Boc-L-Leu-DL-(β-OH)-Phe-OH
  参考文献：
  名称：

  通过动态螺旋的超分子协调对螺旋信息进行手性转录

  摘要：

  以生物学上重要的“肽捆绑”为基序，设计了新的发色环状宿主 1，它由两个锌卟啉单元组成，这些单元通过九聚氨基异丁酸 (Aib) 单元的动态肽螺旋连接。在锌卟啉单元之间包含吡啶锚定螺旋肽后，1 在 410-450 nm 处显示出强烈的激子耦合圆二色性 (CD) 带，其符号反映了客体肽的螺旋意义。对构象定义的含脱氢苯丙氨酸类似物的研究表明，宿主中的动态螺旋链在有限的纳米空间中与客体肽的右手或左手螺旋在立体化学上一致，

  DOI：

  10.1021/ja039369p

文献信息

• Conformational analysis of an active chemotactic peptide analog containing z-dehydrophbnylalanine at position 3
  作者：V.S. Chauhan、Paramjeet Kaur、Nirupa Sen、K. Uma、Jose Jacob、P. Balaram

  DOI：10.1016/s0040-4020(01)81745-2

  日期：1988.1

  of α, β -dehydrophenylalanine on activity and conformation. The analog peptide shows high biological activity in stimulating superoxide production by rabbit neutrophils. An NMR analysis of the solution conformation of the ΔZ-Phe analog, using nuclear Overhauser effects and comparisons with the corresponding saturated peptides, favours a significant population of extended backbone conformations.

  合成了趋化三肽的甲酰-Met-Leu- ΔZ -Phe-OMe甲酰-Met-Leu-Phe，以评估α，β-脱氢苯丙氨酸的取代对活性和构象的影响。类似物肽在刺激兔嗜中性粒细胞产生超氧化物方面显示出高的生物学活性。使用核Overhauser效应对ΔZ -Phe类似物的溶液构象进行NMR分析，并与相应的饱和肽进行比较，这有利于大量的扩展骨架构象。
• Design of peptides with α,β-dehydro-residues: synthesis, crystal structure and molecular conformation of a peptide N-tertiary-butyloxycarbonyl-l-Leu-ΔPhe-L-Ile-OCH3
  作者：V.K. Goel、M. Guha、A.P. Baxla、S. Dey、T.P. Singh

  DOI：10.1016/s0022-2860(03)00464-2

  日期：2003.9

  rules with dehydro-residues a peptide tertiary-butyloxycarbonyl- l -Leu-ΔPhe- l -Ile-OCH 3 was synthesized. The synthesis was carried out in solution using azlactone procedure. The three-dimensional structure of the peptide was determined by X-ray diffraction method and refined to an R -factor of 0.065. The peptide adopts an unfolded S-shaped conformation with φ 1 =−78.8(6)°, ψ 1 =−28.5(7)°, φ 2 =51.8(7)°

  摘要 为了开发具有脱氢残基的新设计规则，合成了肽叔丁氧羰基-1-Leu-ΔPhe-1-Ile-OCH 3 。使用吖内酯程序在溶液中进行合成。肽的三维结构通过X射线衍射法确定并精制至R因子为0.065。该肽采用未折叠的 S 形构象，φ 1 =−78.8(6)°, ψ 1 =−28.5(7)°, φ 2 =51.8(7)°, ψ 2 =44.6(7)°, φ 3 =−93.7(7)°，ψ 3 T =21.5(7)°。这是在 (i+2) 位具有 ΔPhe 且具有单个支链 β-碳残基的肽的特征性未折叠构象的第一个例子。χ 1,1 =60.5(8)° χ 1,2 =-66.7(7)° 的 Ile 侧链构象不是有利的形式，因此导致强烈的空间约束。
• Novel phytotoxic and plant growth regulating oligopeptide
  申请人：The United States of America as represented by the Secretary of

  公开号：US04735651A1

  公开（公告）日：1988-04-05

  The following novel oligopeptide compounds which possess phytotoxic and plant growth regulating properties and methods for their use are disclosed: R.sub.1 -N(R.sub.2)-D,L-Ala-D,L-Leu-N(R.sub.2).DELTA.Phe-Gly-OR.sub.3 ; in which R.sub.1 is H or a protecting group at the amino terminus of the type 9-fluorenylmethoxycarbonyl, or benzyloxycarbonyl, R.sub.2 is an alkyl of 2 to 3 carbon atoms, R.sub.3 is hydrogen or an alkyl of 2 to 3 carbon atoms, and .DELTA.Phe is dehydrophenylalanine. R.sub.1 -D,L-Leu-N(R.sub.4)-.DELTA.Phe-Gly-OR.sub.3 ; R.sub.1 Aib-N(R.sub.2)-.DELTA.Phe-Gly-OR.sub.3 ; R.sub.1 -Ala-N(R.sub.5)-.DELTA.Phe-Gly-OR.sub.3 ; R.sub.1 -Val-N(R.sub.2)-.DELTA.Phe-Gly-OR.sub.3 ; wherein R.sub.1 is H or a protecting group at the amino terminus of the type tert-butyloxycarbonyl-(BOC), 9-fluorenylmethyloxycarbonyl, or benzyloxycarbonyl, R.sub.2 is an alkyl of 1 to 3 carbon atoms, R.sub.3 is hydrogen or an alkyl of 1 to 3 carbon atoms, and .DELTA.Phe is dehydrophenylalanine.

  本发明揭示了具有植物毒性和植物生长调节性能的以下新型寡肽化合物及其使用方法： R.sub.1-N(R.sub.2)-D，L-Ala-D，L-Leu-N(R.sub.2).DELTA.Phe-Gly-OR.sub.3；其中，R.sub.1是氨基末端的保护基，类型为9-芴甲氧羰基或苄氧羰基，或者是氢，R.sub.2是2到3个碳原子的烷基，R.sub.3是氢或2到3个碳原子的烷基，.DELTA.Phe是脱氢苯丙氨酸。 R.sub.1-D，L-Leu-N(R.sub.4)-.DELTA.Phe-Gly-OR.sub.3；R.sub.1 Aib-N(R.sub.2)-.DELTA.Phe-Gly-OR.sub.3；R.sub.1-Ala-N(R.sub.5)-.DELTA.Phe-Gly-OR.sub.3；R.sub.1-Val-N(R.sub.2)-.DELTA.Phe-Gly-OR.sub.3；其中，R.sub.1是氨基末端的保护基，类型为tert-丁氧羰基（BOC）、9-芴甲氧羰基或苄氧羰基，R.sub.2是1到3个碳原子的烷基，R.sub.3是氢或1到3个碳原子的烷基，.DELTA.Phe是脱氢苯丙氨酸。
• C-terminal constrained phenylalanine as a pharmacophoric unit in peptide-based proteasome inhibitors
  作者：Anna Baldisserotto、Mauro Marastoni、Ilaria Lazzari、Claudio Trapella、Riccardo Gavioli、Roberto Tomatis

  DOI：10.1016/j.ejmech.2007.10.002

  日期：2008.7

  Here we report the synthesis and biological properties of peptide-based molecules bearing constrained analogues of phenylalanine at the C-terminal. Compounds were tested as proteasome subunits' inhibitors. Dehydro-peptides showed good inhibition, in particular against trypsin-like (T-L) proteasome activity while some C-terminal Tic-derivatives inhibit only caspase-like activity in enzymatic beta 1 subunits with a certain degree of efficacy. The best analogues of the series demonstrated good resistance to proteolysis and a capacity to permeate the cell membrane. (c) 2007 Elsevier Masson SAS. All rights reserved.
• Design of peptides with α,β-dehydro-residues: syntheses, crystal structures and molecular conformations of two ΔPhe-Trp containing peptides
  作者：R. Vijayaraghavan、J. Makker、P. Kumar、S. Dey、T.P. Singh

  DOI：10.1016/s0022-2860(03)00173-x

  日期：2003.6

  The DeltaPhe-Trp is a newly designed moiety that was found inducing a unique conformation in peptides. The peptides Boc-L-Val-DeltaPhe-L-Trp-OCH3 (I) and Boc-L-Leu-DeltaPhe-L-Trp-OCH3 (II) were synthesized by azlactone method in solution phase. The peptide (I) was crystallized from its solution in ethanol-water mixture in orthorhombic space group P2(1)2(1)2(1) with a = 10.663(3) Angstrom, b = 11.204(3) Angstrom, c = 26.516(10) Angstrom and peptide (II) was crystallized from its solution in acetone in a monoclinic space group P2(1) with a = 9.354(1)Angstrom, b = 11.218(4)Angstrom, c = 15.633(1)Angstrom and beta = 101.83(1). The structures were determined by direct methods. Peptide (I) was refined to an R value of 0.059 for 1554 observed reflections [I greater than or equal to 2sigma (I)] and peptide (II) was refined to an R value of 0.043 for 2920 observed reflections [I greater than or equal to 2sigma (1)]. The structures of peptides (I) and (II) were found to be identical. They formed an unusual type VIa beta-turn conformation which is observed for the first time with a APhe residue at (i + 2) position indicating a unique influence of DeltaPhe-Trp moiety in inducing a reproducible new structure in peptides. (C) 2003 Elsevier Science B.V. All rights reserved.