HKK(thioAc)LM | 1082947-82-7

• 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: HKK(thioAc)LM
• 英文别名: His-Lys-Lys(ε-thioAc)-Leu-Met；H-K-K(ε-thioAc)-L-M；His-Lys-Lys(epsilon-thioAc)-Leu-Met；(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-6-amino-2-[[(2S)-2-amino-3-(1H-imidazol-5-yl)propanoyl]amino]hexanoyl]amino]-6-(ethanethioylamino)hexanoyl]amino]-4-methylpentanoyl]amino]-4-methylsulfanylbutanoic acid
• CAS: 1082947-82-7
• 化学式: C₃₁H₅₅N₉O₆S₂
• 分子量: 713.966
• InChiKey: RPADRBKCRCLQJX-LROMGURASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.9
• 重原子数：
  48
• 可旋转键数：
  25
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.71
• 拓扑面积：
  304
• 氢给体数：
  9
• 氢受体数：
  11

反应信息

• 作为产物：
  描述：

  N²-(((9H-fluoren-9-yl)methoxy)carbonyl)-N⁶-ethanethioyl-L-lysine 、 Fmoc-Met-Wang resin 、 Fmoc-L-亮氨酸 、 N-alpha-芴甲氧羰基-N-epsilon-叔丁氧羰基-L-赖氨酸 、 N-Fmoc-N'-三苯甲基-L-组氨酸 在 哌啶 、 O-(benzotriazol-1-yl)-N,N,N',N'-tetramethyluronium tetrafluoroborate 、 N,N-二异丙基乙胺 作用下， 以 N,N-二甲基甲酰胺 为溶剂， 生成 HKK(thioAc)LM
  参考文献：
  名称：

  N^ϵ-Thioacetyl-Lysine-Containing Tri-, Tetra-, and Pentapeptides as SIRT1 and SIRT2 Inhibitors

  摘要：

  N-epsilon-Thioacetyl-lysine-containing tri-, tetra-, and pentapeptides, based on the (x-tubulin and p53 protein sequences, were studied as SIRT1 and SIRT2 inhibitors. The potency of the pentapeptides depended on the selection of the side chains. The removal of N- and C-terminal residues of the pentapeptides; yielded tripeptides with retained SIRT1 inhibitory activity but decreased SIRT2 inhibitory activity. The most potent SIRT1 inhibitors were equipotent with the reference compound (6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide) with the IC50 values of 180-330 nM.

  DOI：

  10.1021/jm801401k

文献信息

• <i>N</i>^ϵ-Thioacetyl-Lysine-Containing Tri-, Tetra-, and Pentapeptides as SIRT1 and SIRT2 Inhibitors
  作者：Päivi H. Kiviranta、Tiina Suuronen、Erik A. A. Wallén、Jukka Leppänen、Jussi Tervonen、Sergiy Kyrylenko、Antero Salminen、Antti Poso、Elina M. Jarho

  DOI：10.1021/jm801401k

  日期：2009.4.9

  N-epsilon-Thioacetyl-lysine-containing tri-, tetra-, and pentapeptides, based on the (x-tubulin and p53 protein sequences, were studied as SIRT1 and SIRT2 inhibitors. The potency of the pentapeptides depended on the selection of the side chains. The removal of N- and C-terminal residues of the pentapeptides; yielded tripeptides with retained SIRT1 inhibitory activity but decreased SIRT2 inhibitory activity. The most potent SIRT1 inhibitors were equipotent with the reference compound (6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1-carboxamide) with the IC50 values of 180-330 nM.