N-acetyl-L-valyl-L-valine methyl ester | 13795-43-2

• 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: N-acetyl-L-valyl-L-valine methyl ester
• 英文别名: Ac-Val-Val-OMe；AcNH-Val-Val-CO2Me；methyl (2S)-2-[[(2S)-2-acetamido-3-methylbutanoyl]amino]-3-methylbutanoate
• CAS: 13795-43-2
• 化学式: C₁₃H₂₄N₂O₄
• 分子量: 272.345
• InChiKey: ZANAAPNWWXNRHK-QWRGUYRKSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.7
• 重原子数：
  19
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.77
• 拓扑面积：
  84.5
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-acetyl-L-valyl-L-valine methyl ester 在 lithium hydroxide 作用下， 以 四氢呋喃 、 水 为溶剂， 生成 Ac-Val-Val-OH
  参考文献：
  名称：

  空气污染物NO2介导的肽主链的碎片化-重排。

  摘要：

  由二氧化氮NO 2介导的肽主链的断裂-重排。，使用二- ，三-探索，和四肽8 - 18作为模型系统。该反应是通过肽键的非自由基N-亚硝化反应引发的，该反应通过排出一个氨基酸部分而缩短了肽链，同时通过形成新的肽键将剩余的分子末端融合在一起。片段化-重排的相对速率取决于氨基酸的性质，并随着α碳上空间体积的增加而降低，顺序为Gly> Ala> Val。具有连续的芳香族侧链的肽仅产生了由于空间上较少拥挤的N末端酰胺的亚硝化而产生的产物。这样的骨架断裂-重排发生在生理相关条件下，并且可能是肽的重要反应途径，其中没有容易氧化的侧链的部分暴露于空气污染物NO2 。。除了NO 2 。-诱导的自由基氧化过程，这一结果表明，在评估NO 2时应考虑离子反应途径，特别是亚硝化作用。在生物系统中的反应性。

  DOI：

  10.1002/chem.201501850
• 作为产物：
  描述：

  methyl (2S)-2-[(2-acetamido-3-methylbutanoyl)amino]-3-methylbutanoate 生成 N-acetyl-L-valyl-L-valine methyl ester
  参考文献：
  名称：

  MIYAZAWA, TOSHIFUMI;YAMADA, TAKASHI;KUWATA, SHIGERU, CHEM. EXPRESS., 6,(1991) N, C. 137-140

  摘要：

  DOI：

文献信息

• Determining the Diastereoselectivity of the Formation of Dipeptidonucleotides by NMR Spectroscopy
  作者：Olivia Doppleb、Jennifer Bremer、Maren Bechthold、Carolina Sánchez Rico、Daniela Göhringer、Helmut Griesser、Clemens Richert

  DOI：10.1002/chem.202101630

  日期：2021.9.24

  as building blocks. It is interesting to ask whether this is a coincidence or a consequence of the functional interplay of these biomolecules. One reaction that provides an opportunity to study this interplay is the formation of phosphoramidate-linked peptido RNA from amino acids and ribonucleotides in aqueous condensation buffer. Here we report how the diastereoselectivity of the first peptide coupling

  蛋白质由l-氨基酸组成，但核酸和大多数寡糖含有d-糖作为构建块。有趣的是要问这是巧合还是这些生物分子功能相互作用的结果。为研究这种相互作用提供机会的一个反应是在水性缩合缓冲液中由氨基酸和核糖核苷酸形成氨基磷酸酯连接的肽 RNA。在这里，我们报告了如何通过 NMR 光谱原位确定肽 RNA 途径的第一个肽偶联的非对映选择性。当氨基酸酯的外消旋混合物与 5'-氨基酸基核苷酸反应时，通过整合31 P-或1 H-NMR峰。发现同手性偶联产物d -Ser - d -Trp 的非对映体过量最高，氨基磷酸酯通过其d-核糖环与腺苷 5'-单磷酸相连。当用N控制反应时-乙酰氨基酸和缬氨酸甲酯在有机溶剂中运行，发现非对映选择性较低，非对映比≤62:38。因此探索性研究的结果表明，核糖核苷酸残基不仅促进了亲脂性氨基的偶联水介质中的酸，但也形成同手性二肽。此处描述的方法可用于搜索揭示同手性起源的其他立体选择性反应。
• Synthesis of (3<i>S</i>, 4<i>S</i>)- and (3<i>S</i>, 4<i>R</i>)-4-Amino-3-hydroxy-6-methylheptanoic Acid, and Their<i>N</i>-(Acetyl-L-valyl-L-valyl) Derivatives
  作者：Mitsuhiro Kinoshita、Akito Hagiwara、Shinpei Aburaki

  DOI：10.1246/bcsj.48.570

  日期：1975.2

  ptanoic acid (10a) present in pepstatins, specific inhibitors of acid proteases, and its (+) (3S,4R) diastereomer (10b) were synthesized starting from 3-deoxy-1,2-O-isopropylidene-α-D-erythro-pentodialdo-1,4-furanose (1) through highly stereoselective and stereospecific routes. The partial pep tide of pepstatin Ac, N-(acetyl-L-valyl-L-valyl)-(3S,4S)-4-amino-3-hydroxy-6-methylheptanoic acid (15a) and

  存在于胃蛋白酶抑制剂、酸性蛋白酶的特异性抑制剂及其 (+) (3S,4R) 非对映异构体 (10b) 中的天然 (-)(3S,4S)-4-氨基-3-羟基-6-inethylheptanoic 酸 (10a) 是从 3-deoxy-1,2-O-isopropylidene-α-D-erythro-pentodialdo-1,4-furanose (1) 通过高度立体选择性和立体特异性路线合成。胃酶抑素Ac、N-(乙酰基-L-缬氨酰-L-缬氨酰)-(3S,4S)-4-氨基-3-羟基-6-甲基庚酸(15a)及其(3S,4R)的部分肽非对映异构体 (15b) 是通过 10a 和 10b 的叔丁酯分别与乙酰基-L-缬氨酰-L-缬氨酸叠氮化物的叠氮偶联合成的。化合物15a抑制胃蛋白酶的蛋白水解，然而，非对映异构体15b对胃蛋白酶没有抑制作用。
• Intermolecular β-Sheet Stabilization with Aminopyrazoles
  作者：Christian N. Kirsten、Thomas H. Schrader

  DOI：10.1021/ja972158y

  日期：1997.12.17

  3-Aminopyrazole derivatives are the first artificial templates that stabilize the beta-sheet conformation in N/C-protected dipeptides by purely intermolecular interactions. In the complex two aminopyrazole molecules lie exactly above and below the peptide backbone. Binding to the top face of the peptide is strongly favored because it forms three cooperative hydrogen bonds simultaneously to the receptor molecule, whereas the bottom face has only two. Polymerizable 3-amino- and 3-amidopyrazoles have been made accessible in excellent yields by a general route starting from p-toluic acid. With H-1 NMR titrations binding constants for the 1:1 complex of up to 880 M-1 have been determined in chloroform. The association constants are strongly influenced by the electronic character of the aminopyrazole derivative as well as by the steric demand of the peptide residues. Variable temperature studies prove that the complex is formed by dynamic hydrogen bonds and confirmed the preferential binding of the receptor molecules at the top face. By detailed Karplus-analysis of the NH-alpha-CH coupling constants in the complex a remarkable correlation between the dihedral angle theta and the degree of complexation was found, which shows that several amidopyrazoles are capable of forcing the dipeptide into an almost ideal P-sheet conformation. In glycine-containing dipeptides the third hydrogen bond slows down the free rotation around the C-C/C-N bond to almost zero. Intramolecular nuclear Overhauser enhancements (NOE) provide additional evidence for the peptide's extended conformation, while strong reciprocal intermolecular NOEs give the final proof of the existence of the critical third hydrogen bond and the postulated mutual orientation of the complexation partners. First H-1 NMR titrations with tripeptides show very promising results concerning the application of this concept to oligopeptides.
• The nucleation of monomeric parallel β-sheet-like structures and their self-assembly in aqueous solution
  作者：Penchit Chitnumsub、Wayne R. Fiori、Hilal A. Lashuel、Humberto Diaz、Jeffery W. Kelly

  DOI：10.1016/s0968-0896(98)00222-3

  日期：1999.1

  The aromatic diacid residue 4,6-dibenzofuranbispropionic acid (1) was designed to nucleate a parallel beta-sheet-like structure in small peptides in aqueous solution via a hydrogen-bonded hydrophobic cluster. Even though a 14-membered ring hydrogen bond necessary for parallel beta-sheet formation is favored in simple amides composed of 1, this hydrogen bonding interaction does not appear to be sufficient to nucleate parallel beta-sheet formation in the absence of hydrophobic clustering between the dibenzofuran portion of 1 and the hydrophobic side chains of the flanking alpha-amino acids. The subsequence --hydrophobic residue-1-hydrophobic residue-- is required for folding in the context of a nucleated two-stranded parallel beta-sheet structure. In all cases where the peptidomimetics can fold into two diastereomeric parallel beta-sheet structures having different hydrogen bonding networks, these conformations appear to exchange rapidly. The majority of the parallel beta-sheet structures evaluated herein undergo linked intramolecular folding and self-assembly, affording a fibrillar beta-sheet quaternary structure. To unlink folding and assembly, asymmetric parallel beta-sheet structures incorporating N-methylated alpha-amino acid residues have been synthesized using a new solid phase approach. Residue 1 facilitates the folding of several peptides described within affording a monomeric parallel beta-sheet-like structure in aqueous solution, as ascertained by a variety of spectroscopic and biophysical methods, increasing our understanding of parallel beta-sheet structure.
• MIYAZAWA, TOSHIFUMI;YAMADA, TAKASHI;KUWATA, SHIGERU, CHEM. EXPRESS., 6,(1991) N, C. 137-140
  作者：MIYAZAWA, TOSHIFUMI、YAMADA, TAKASHI、KUWATA, SHIGERU

  DOI：——

  日期：——