Fmoc-Lys(cr)-OH | 1245942-53-3

• 分子结构分类: 有机化合物 - 苯类化合物 - 芴
• 英文名称: Fmoc-Lys(cr)-OH
• 英文别名: (S,E)-2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-6-but-2-enamidohexanoic acid；Fmoc-Lys(Crotonyl)-OH；(2S)-6-[[(E)-but-2-enoyl]amino]-2-(9H-fluoren-9-ylmethoxycarbonylamino)hexanoic acid
• CAS: 1245942-53-3
• 化学式: C₂₅H₂₈N₂O₅
• 分子量: 436.508
• InChiKey: WFNXIABNUWPOIE-INZNARQDSA-N

物化性质

• 沸点：
  725.2±60.0 °C(Predicted)
• 密度：
  1.219±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  3.9
• 重原子数：
  32
• 可旋转键数：
  11
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.32
• 拓扑面积：
  105
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  甲醇 、 、 Fmoc-Lys(cr)-OH 、 Fmoc-L-丙氨酸 、 溶剂黄146 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， 反应 1.25h， 以76%的产率得到(S)-methyl 2-((S)-2-((S)-2-acetamidopropanamido)-6-((E)-but-2-enamido)hexanamido)propanoate
  参考文献：
  名称：

  Nε-Modified lysine containing inhibitors for SIRT1 and SIRT2

  摘要：

  Sirtuins catalyze the NAD(+) dependent deacetylation of N-epsilon-acetyl lysine residues to nicotinamide, O '-acetyl- ADP-ribose (OAADPR) and N-epsilon-deacetylated lysine. Here, an easy-to-synthesize Ac-Ala-Lys-Ala sequence has been used as a probe for the screening of novel N-epsilon-modified lysine containing inhibitors against SIRT1 and SIRT2. N-epsilon-Selenoacetyl and N-epsilon-isothiovaleryl were the most potent moieties found in this study, comparable to the widely studied N-epsilon-thioacetyl group. The N-epsilon-3,3-dimethylacryl and N-epsilon-isovaleryl moieties gave significant inhibition in comparison to the N-epsilon-acetyl group present in the substrates. In addition, the studied N-epsilon-alkanoyl, N-epsilon-alpha,beta-unsaturated carbonyl and N-epsilon-aroyl moieties showed that the acetyl binding pocket can accept rather large groups, but is sensitive to even small changes in electronic and steric properties of the N-epsilon-modification. These results are applicable for further screening of Ne-acetyl analogues. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2010.06.035
• 作为产物：
  描述：

  (S,E)-methyl 2-(((9H-fluoren-9-yl)methoxy)carbonylamino)-6-but-2-enamidohexanoate 在 水 、 calcium chloride 、 sodium hydroxide 、 溶剂黄146 作用下， 以 异丙醇 、 水 为溶剂， 反应 3.0h， 以84%的产率得到Fmoc-Lys(cr)-OH
  参考文献：
  名称：

  Nε-Modified lysine containing inhibitors for SIRT1 and SIRT2

  摘要：

  Sirtuins catalyze the NAD(+) dependent deacetylation of N-epsilon-acetyl lysine residues to nicotinamide, O '-acetyl- ADP-ribose (OAADPR) and N-epsilon-deacetylated lysine. Here, an easy-to-synthesize Ac-Ala-Lys-Ala sequence has been used as a probe for the screening of novel N-epsilon-modified lysine containing inhibitors against SIRT1 and SIRT2. N-epsilon-Selenoacetyl and N-epsilon-isothiovaleryl were the most potent moieties found in this study, comparable to the widely studied N-epsilon-thioacetyl group. The N-epsilon-3,3-dimethylacryl and N-epsilon-isovaleryl moieties gave significant inhibition in comparison to the N-epsilon-acetyl group present in the substrates. In addition, the studied N-epsilon-alkanoyl, N-epsilon-alpha,beta-unsaturated carbonyl and N-epsilon-aroyl moieties showed that the acetyl binding pocket can accept rather large groups, but is sensitive to even small changes in electronic and steric properties of the N-epsilon-modification. These results are applicable for further screening of Ne-acetyl analogues. (C) 2010 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2010.06.035

文献信息

• Peptide‐Based Fluorescent Probes for Deacetylase and Decrotonylase Activity: Toward a General Platform for Real‐Time Detection of Lysine Deacylation
  作者：Debra R. Rooker、Yuliya Klyubka、Ritika Gautam、Elisa Tomat、Daniela Buccella

  DOI：10.1002/cbic.201700582

  日期：2018.3.2

  deacetylases can remove other acyl modifications on lysines, the roles and regulation of which are far less understood. A versatile peptide‐based fluorescent probe for single‐reagent, real‐time detection of deacetylase activity that can be readily adapted for probing broader lysine deacylation is described.

  一个独特的平台，不同的PTM：除乙酰基外，脱乙酰基酶还可以去除赖氨酸上的其他酰基修饰，其作用和调控尚不清楚。本文介绍了一种基于肽的多功能荧光探针，可用于单试剂，实时检测脱乙酰酶活性，可以很容易地用于检测更广泛的赖氨酸脱酰作用。