Nps-Lys(Fmoc)-OH | 135523-68-1

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: Nps-Lys(Fmoc)-OH
• CAS: 135523-68-1
• 化学式: C₂₇H₂₇N₃O₆S
• 分子量: 521.594
• InChiKey: UTKXOMPCTMWRJT-QHCPKHFHSA-N

物化性质

• 密度：
  1.39±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  5.35
• 重原子数：
  37.0
• 可旋转键数：
  12.0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.26
• 拓扑面积：
  130.8
• 氢给体数：
  3.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  Nps-Lys(Fmoc)-OH 在 盐酸 、 1-羟基苯并三唑 、 二乙胺 、 三乙胺 、 N,N'-二环己基碳二亚胺 作用下， 以 乙醚 、 氯仿 、 N,N-二甲基甲酰胺 为溶剂， 反应 26.66h， 生成 benzyl N-[(2S)-1-[[(2S)-1-[[2-[[(2S)-6-amino-1-[(9-ethylcarbazol-3-yl)amino]-1-oxohexan-2-yl]amino]-2-oxoethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]carbamate
  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：

  N'-Fmoc-L-赖氨酸 、 2-硝基苯硫氯 在 sodium hydroxide 作用下， 以 1,4-二氧六环 为溶剂， 以91%的产率得到Nps-Lys(Fmoc)-OH
  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