H-L-Ala-L-Ala-L-Ala-OBzl.HCl | 77935-62-7

• 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: H-L-Ala-L-Ala-L-Ala-OBzl.HCl
• CAS: 77935-62-7
• 化学式: C₁₆H₂₃N₃O₄*ClH
• 分子量: 357.837
• InChiKey: NDDOPKSZRZBAFU-LFELFHSZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  0.51
• 重原子数：
  24.0
• 可旋转键数：
  7.0
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.44
• 拓扑面积：
  110.52
• 氢给体数：
  3.0
• 氢受体数：
  5.0

反应信息

• 作为反应物：
  描述：

  H-L-Ala-L-Ala-L-Ala-OBzl.HCl 在 palladium on activated charcoal 氢气 、 三乙胺 作用下， 以 甲醇 、 水 、 二甲基亚砜 、 N,N-二甲基甲酰胺 为溶剂， 反应 54.0h， 生成
  参考文献：
  名称：

  Peptide derivatives specific for a Plasmodium falciparum proteinase inhibit the human erythrocyte invasion by merozoites

  摘要：

  A specific proteinase of P. falciparum merozoites has been detected by using hydrosoluble fluorogenic peptidic substrates synthesized by classical peptide chemistry; their N-terminal end was acylated by a gluconoyl group that protects them from aminopeptidase degradation and increases their hydrosolubility, and their carboxylic end was substituted by a 3-amino-9-ethylcarbazole group. The sequence Val-Leu-Gly-Lys was found to be the most specific substrate. On this basis, reversible peptidic inhibitors were synthesized by substituting the C-terminal lysyl residue, at the proteolytic site, by different alkylamines and amino alcohols. The activity of these compounds, studied on the P. falciparum proteinase and in in vitro cultures, strongly suggests a specific effect of this peptidic sequence on the reinvasion process. The peptidic inhibitors do not impair the release of merozoites from schizonts, but selectively inhibit the invasion step leading to the formation of rings. Although the natural target of this enzyme is not yet known, these specific peptide inhibitors could lead to a new antimalarial approach.

  DOI：

  10.1021/jm00114a011
• 作为产物：
  描述：

  在 盐酸 、 N,N'-二环己基碳二亚胺 作用下， 以 乙醚 、 乙酸乙酯 、 丙酮 为溶剂， 反应 28.66h， 生成 H-L-Ala-L-Ala-L-Ala-OBzl.HCl
  参考文献：
  名称：

  Peptide derivatives specific for a Plasmodium falciparum proteinase inhibit the human erythrocyte invasion by merozoites

  摘要：

  A specific proteinase of P. falciparum merozoites has been detected by using hydrosoluble fluorogenic peptidic substrates synthesized by classical peptide chemistry; their N-terminal end was acylated by a gluconoyl group that protects them from aminopeptidase degradation and increases their hydrosolubility, and their carboxylic end was substituted by a 3-amino-9-ethylcarbazole group. The sequence Val-Leu-Gly-Lys was found to be the most specific substrate. On this basis, reversible peptidic inhibitors were synthesized by substituting the C-terminal lysyl residue, at the proteolytic site, by different alkylamines and amino alcohols. The activity of these compounds, studied on the P. falciparum proteinase and in in vitro cultures, strongly suggests a specific effect of this peptidic sequence on the reinvasion process. The peptidic inhibitors do not impair the release of merozoites from schizonts, but selectively inhibit the invasion step leading to the formation of rings. Although the natural target of this enzyme is not yet known, these specific peptide inhibitors could lead to a new antimalarial approach.

  DOI：

  10.1021/jm00114a011

文献信息

• Synthesis and antibacterial activities of theanine-containing oligopeptides.
  作者：YASUO ODA、HIROKO TAGUCHI、NOBUTAKA MASAOKA、KAZUO MINAMI、SUSUMU HONDA、KOZO OKADA

  DOI：10.1248/cpb.28.3549

  日期：——

  Theanine, an antimetabolite of L-glutamic acid, is a weak antibacterial agent. In the hope of obtaining theanine derivatives which have more potent biological activities, a series of theanyl-L-alanine oligopeptides, H-Tea-L-Alan-OH (n=1, 2, 3), and several derivatives of these peptides with blocking groups at the amono-and/or carboxyl-termini were prepared, and their antibacterial and anti-glutamic decarboxylase activities were examined. Theanyl-L-alanine and theanyl-L-alanyl-L-alanine inhibited the growth of Staphylococcus aureus and Escherichia coli most strongly, the percent inhibitions being 2 to 23 times higher against S. aureus or 3 to 4 times higher against E. coli than those of theanine. Structural modifications at the end groups of the peptides, especially N-acylation, caused marked reductions in the antibacterial activities. None of the theanine and theanyl-L-alanine oligopeptides possessed any significant ability to inhibit bacterial glutamic decarboxylase even at a concentration of 50 μmol/ml.

  茶氨酸是 L-谷氨酸的一种抗代谢物，是一种弱抗菌剂。为了获得具有更强生物活性的茶氨酸衍生物，我们制备了一系列茶氨酸-L-丙氨酸寡肽 H-Tea-L-Alan-OH（n=1、2、3），以及这些肽在氨基端和/或羧基端带有阻断基团的几种衍生物，并研究了它们的抗菌和抗谷氨酸脱羧酶活性。丙氨酰-L-丙氨酸和丙氨酰-L-丙氨酰-L-丙氨酸对金黄色葡萄球菌和大肠杆菌的抑制作用最强，对金黄色葡萄球菌的抑制率是丙氨酸的 2 至 23 倍，对大肠杆菌的抑制率是丙氨酸的 3 至 4 倍。肽末端基团的结构修饰，尤其是 N-酰化，会明显降低抗菌活性。即使在 50 μmol/ml 的浓度下，也没有任何一种茶氨酸和茶氨酸-L-丙氨酸寡肽具有明显的抑制细菌谷氨酸脱羧酶的能力。
• Peptide derivatives specific for a Plasmodium falciparum proteinase inhibit the human erythrocyte invasion by merozoites
  作者：Roger Mayer、Isabelle Picard、Philippe Lawton、Philippe Grellier、Christine Barrault、Michel Monsigny、Joseph Schrevel

  DOI：10.1021/jm00114a011

  日期：1991.10

  A specific proteinase of P. falciparum merozoites has been detected by using hydrosoluble fluorogenic peptidic substrates synthesized by classical peptide chemistry; their N-terminal end was acylated by a gluconoyl group that protects them from aminopeptidase degradation and increases their hydrosolubility, and their carboxylic end was substituted by a 3-amino-9-ethylcarbazole group. The sequence Val-Leu-Gly-Lys was found to be the most specific substrate. On this basis, reversible peptidic inhibitors were synthesized by substituting the C-terminal lysyl residue, at the proteolytic site, by different alkylamines and amino alcohols. The activity of these compounds, studied on the P. falciparum proteinase and in in vitro cultures, strongly suggests a specific effect of this peptidic sequence on the reinvasion process. The peptidic inhibitors do not impair the release of merozoites from schizonts, but selectively inhibit the invasion step leading to the formation of rings. Although the natural target of this enzyme is not yet known, these specific peptide inhibitors could lead to a new antimalarial approach.