D-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酸 | 10251-27-1

• 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
• 中文名称: D-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酸
• 英文名称: hexaalanine
• 英文别名: AAAAAA；Ala6；A6；Ala₆；L-alanyl=>L-alanyl=>L-alanyl=>L-alanyl=>L-alanyl=>-L-alanine；H-Ala-Ala-Ala-Ala-Ala-Ala-OH；(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-aminopropanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]propanoyl]amino]propanoic acid
• CAS: 10251-27-1；10251-28-2；10251-30-6；10251-31-7；10251-32-8；10413-79-3；10576-91-7
• 化学式: C₁₈H₃₂N₆O₇
• 分子量: 444.488
• InChiKey: ZLHDFPIXRRJBKM-ZNSCXOEOSA-N

物化性质

• 沸点：
  929.2±65.0 °C(Predicted)
• 密度：
  1.248±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -4.3
• 重原子数：
  31
• 可旋转键数：
  11
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  209
• 氢给体数：
  7
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  D-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酸 在 sodium hypochlorite 作用下， 以 phosphate buffer 为溶剂， 反应 0.17h， 生成 N-chlorohexaalanine
  参考文献：
  名称：

  Rates of Reduction of N-Chlorinated Peptides by Sulfite:  Relevance to Incomplete Dechlorination of Wastewaters

  摘要：

  Biologically induced fragmentation of proteins during wastewater treatment produces peptides, which form long-lasting organic chloramines when the water is disinfected with Cl-2. To protect aquatic wildlife from residual chlorine, including chloramines, wastewaters are often treated with sulfur dioxide or sulfite salts. This strategy incompletely eliminates residual chlorine species. Here we report that dechlorination rate constants of N-chloropeptides are 1-2 order of magnitude smaller than those for NH2Cl and some aliphatic organic chloramines. Slow rates explain the prevalence of N-chloropeptides in dechlorinated wastewaters after faster reacting chlorine species have been eliminated. Dechlorination is subject to general acid catalysis. For N-chlorinated leucylalanine, the rate law above pH 6 in phosphate buffer at 25 degrees C and I approximate to 0.1 M is as follows: rate = (9.92 +/- 0.41 x 10(3)[H2PO4-] + 5.70 +/- 0.52 x 10(8)[H3O+] + 5.3 +/- 0.2)[SO32-][Cl-Leu-Ala] (concentrations in M, time in s). Rate constants for other peptides appear to be of similar magnitude; variations in the acid-catalyzed terms among different hydrophobic peptides correlate with solvation energies of side chains. The kinetic data suggest that reducing N-chloropeptides in wastewaters by 75% or more will require reaction times generally >0.5 h at environmentally acceptable S-IV doses and pH values.

  DOI：

  10.1021/es9707365
• 作为产物：
  描述：

  tetra-L-alanine 在 sodium hydroxide 、 氨 、 水 、 lithium bromide 作用下， 生成 D-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酰-L-丙氨酸
  参考文献：
  名称：

  Abderhalden; Gohdes, Fermentforschung, 1931, vol. 13, p. 55

  摘要：

  DOI：

文献信息

• Mechanism study on the Oligomerization of Amino Acids into Peptides by Phosphorus Trichloride
  作者：Wenjie Zhao、Dongxin Zhao、Kui Lu

  DOI：10.1080/10426500701807467

  日期：2008.1.14

  As treated by phosphorus trichloride, amino acids could oligomerize into polypeptides. Based on the results obtained by 31P-NMR and ESI-MS/MS, a possible reaction mechanism was proposed. The mechanism might undergo a penta-coordinated phosphorus intermediat. The activated amino acid was a five-membered cyclic penta-coordinated phosphorus intermediate. The nucleophilic attack of the amino group from

  经三氯化磷处理后，氨基酸可寡聚化为多肽。基于31P-NMR和ESI-MS/MS的结果，提出了可能的反应机理。该机制可能会经历五配位的磷中间体。活化的氨基酸是五元环状五配位磷中间体。氨基酸或肽的氨基对中间体羰基的亲核攻击导致肽的形成并释放出一当量的二氯化磷酸。反应序列的重复产生了一系列寡肽。
• Asymmetric epoxidation of electron-poor olefins-V
  作者：Stefano Banfi、Stefano Colonna、Henriette Molinari、Sebastian Julia、Joan Guixer

  DOI：10.1016/s0040-4020(01)91272-4

  日期：1984.1

  New poly-α-aminoacids modified at the C orN-terminal groups are synthetised and employed in the asymmetric epoxidation of chalcone. Their influence on the stereoselectivity of the reaction is studied.

  合成了在C或N端基团上修饰的新的聚α-氨基酸，并将其用于查尔酮的不对称环氧化中。研究了它们对反应立体选择性的影响。
• Structure and Dynamics of the Homologous Series of Alanine Peptides:  A Joint Molecular Dynamics/NMR Study
  作者：Jürgen Graf、Phuong H. Nguyen、Gerhard Stock、Harald Schwalbe

  DOI：10.1021/ja0660406

  日期：2007.2.1

  The phi,psi backbone angle distribution of small homopolymeric model peptides is investigated by a joint molecular dynamics (MD) simulation and heteronuclear NMR study. Combining the accuracy of the measured scalar coupling constants and the atomistic detail of the all-atom MD simulations with explicit solvent, the thermal populations of the peptide conformational states are determined with an uncertainty of < 5 %. Trialanine samples mainly (similar to 90%) a poly-L-proline II helix-like structure, some (similar to 10%) beta extended structure, but no alpha(R) helical conformations. No significant change in the distribution of conformers is observed with increasing chain length (Ala(3) to Ala(7)). Trivaline samples all three major conformations significantly. Tryglycine samples the four corner regions of the Ramachandran space and exists in a slow conformational equilibrium between the cis and trans conformation of peptide bonds. The backbone angle distribution was also studied for the segment Ala(3) surrounded by either three or eight amino acids on both N- and C-termini from a sequence derived from the protein hen egg white lysozyme. While the conformational distribution of the central three alanine residues in the 9mer is similar to that for the small peptides Ala(3)-Ala(7,) major differences are found for the 19mer, which significantly (30-40%) samples alpha(R) helical stuctures.
• Optical Rotation of Peptides. V. Alanine Tetra-, Penta- and Hexapeptides¹
  作者：Erwin Brand、Bernard F. Erlanger、Howard Sachs

  DOI：10.1021/ja01127a505

  日期：1952.4
• Aminopeptidase
  申请人：CAMPINA MELKUNIE B.V.

  公开号：EP0415470B1

  公开（公告）日：1995-01-04