γ⁴(R)Val-OH*HCl | 1451008-49-3

• 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: γ⁴(R)Val-OH*HCl
• CAS: 1451008-49-3
• 化学式: C₈H₁₇NO₂*ClH
• 分子量: 195.689
• InChiKey: MGHWUUBFULWPQJ-OGFXRTJISA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.34
• 重原子数：
  12.0
• 可旋转键数：
  4.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  52.32
• 氢给体数：
  1.0
• 氢受体数：
  3.0

反应信息

• 作为反应物：
  描述：

  γ⁴(R)Val-OH*HCl 在 N-甲基吗啉 、 甲酸 、 氯甲酸异丁酯 作用下， 以 二氯甲烷 为溶剂， 生成 H-[γ4(R)Val]2-OMe
  参考文献：
  名称：

  Unconstrained Homooligomeric γ-Peptides Show High Propensity for C₁₄ Helix Formation

  摘要：

  Monosubstituted gamma(4)-residues (gamma(4)Leu, gamma(4)Ile, and gamma(4)Val) form helices even in short homooligomeric sequences. C-14 helix formation is established by X-ray diffraction in homooligomeric (gamma)(n) tetra-, hexa- and decapeptide sequences demonstrating the high propensity of gamma residues, with proteinogenic side chains, to adopt locally folded conformations.

  DOI：

  10.1021/ol402248s

文献信息

• C₁₂-Helix Development in (αγ)<i>_n</i>Sequences - Spectroscopic Characterization of Boc-[Aib-γ⁴(<i>R</i>)Val]-OMe Oligomers
  作者：Bhimareddy Dinesh、Vishwanathan Vinaya、Srinivasarao Raghothama、Padmanabhan Balaram

  DOI：10.1002/ejoc.201300264

  日期：2013.6

  Boc-Aib-4(R)Val]n-OMe (n = 1-8) in organic solvents have been probed by NMR, IR, and CD spectroscopic methods. In the solid state, this peptide series favors C12-helical conformations, which are backbone-expanded analogues of 310 helices in -peptide sequences. NMR studies of the six- (n = 3) and 16-residue (n = 8) peptides reveal that only two NH protons attached the N-terminus residues Aib(1) and 4(R)Val(2)

  已通过 NMR、IR 和 CD 光谱方法探测了杂合寡肽 Boc-Aib-4(R)Val]n-OMe (n = 1-8) 在有机溶剂中的溶液构象。在固态下，该肽系列有利于 C12 螺旋构象，它是肽序列中 310 个螺旋的骨架扩展类似物。6- (n = 3) 和 16-残基 (n = 8) 肽的 NMR 研究表明，只有两个 NH 质子连接到 N 末端残基 Aib(1) 和 4(R)Val(2) 是溶剂暴露的. 在残基处也观察到具有局部螺旋构象特征的连续 NiH-Ni+1H NOE。IR 研究表明，链延长导致氢键 NH 伸缩带 (3343-3280 cm-1) 的强度大幅增强，这表明分子内氢键结构的伸长。NMR 和 IR 观察结果支持序列延长后 C12 螺旋结构的发展。()n 肽的 CD 谱显示在约 2 处为负最大值。206 nm 和在约的正最大值。192 nm，光谱特征与 β 肽中的 310 个螺旋不同。
• Structural characterization of folded and extended conformations in peptides containing γ amino acids with proteinogenic side chains: crystal structures of γ_n, (αγ)_n and γγδγ sequences
  作者：Madhusudana M. B. Reddy、K. Basuroy、S. Chandrappa、B. Dinesh、B. Vasantha、Manjunath A. Venkatesha、P. Balaram

  DOI：10.1039/c5nj00132c

  日期：——

  successive C12 hydrogen bonds. γ4Val residues have also been incorporated into the strand segments of a crystalline octapeptide, Boc-Leu-γ4(R)Val-Val-DPro-Gly-Leu-γ4(R)Val-Val-OMe 8. The γγδγ tetrapeptide containing γ4Val and δ5Leu residues adopts an extended sheet like structure. The hydrogen bonding pattern at γ residues corresponds to an apolar sheet, while a polar sheet is observed at the lone δ residue

  含有γ9种肽的晶体结构4的Val和γ 4中描述亮氨酸。该短序列的Boc- [γ 4（[R ）缬氨酸] 2 -OMe 1，将Boc- [γ 4（[R ）缬氨酸] 3 -NHMe 2和Boc-γ 4（小号）的Val-γ 4（[R ）的Val-OME 3采用扩展的非极性，片状结构。所述四肽的Boc- [γ 4（[R ）缬氨酸] 4 -OMe 4采用伸展构象，相对于所述折叠Ç 14螺旋结构先前针对的Boc- [γ确定4（[R ）亮氨酸] 4 -OMe。混合动力αγ序列的Boc- [丙氨酸- γ 4（[R ）亮氨酸] 2 -OMe 5采用的分子内氢键的S形结构缺乏，与两个α残采用本地螺旋构象。与之形成鲜明对比，所述四肽的Boc- [AIB-γ 4（小号）亮氨酸] 2 -OMe 6和的Boc- [LEU-γ 4（[R ）亮氨酸] 2 -OMe 7采用由两个连续的下稳定的折叠结构12氢键。γ 4缬氨酸残
• C₁₂ Helices in Long Hybrid (αγ)_<i>n</i> Peptides Composed Entirely of Unconstrained Residues with Proteinogenic Side Chains
  作者：Rajesh Sonti、Bhimareddy Dinesh、Krishnayan Basuroy、Srinivasarao Raghothama、Narayanaswamy Shamala、Padmanabhan Balaram

  DOI：10.1021/ol500307p

  日期：2014.3.21

  Unconstrained gamma(4) amino acid residues derived by homologation of proteinogenic amino acids facilitate helical folding in hybrid (alpha gamma)(n) sequences. The C-12 helical conformation for the decapeptide, Boc-[Leu-gamma(4)(R)Val](5)-OMe, is established in crystals by X-ray diffraction. A regular C-12 helix is demonstrated by NMR studies of the 18 residue peptide, Boc-[Leu-gamma(4)(AR)Val](9)-OMe, and a designed 16 residue (alpha gamma)(n) peptide, incorporating variable side chains. Unconstrained (alpha gamma)(n) peptides show an unexpectedly high propensity for helical folding in long polypeptide sequences.