1-butyl-1-methyl-2-oxopyrrolidinium bromide | 1583305-29-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 哌啶类
• 英文名称: 1-butyl-1-methyl-2-oxopyrrolidinium bromide
• 英文别名: N-butyl-N-methyl-2-oxopyrrolidinium bromide；1-Butyl-1-methylpyrrolidonium bromide；1-butyl-1-methylpyrrolidin-1-ium-2-one;bromide
• CAS: 1583305-29-6
• 化学式: Br*C₉H₁₈NO
• 分子量: 236.152
• InChiKey: GRSBKKMTYONWLB-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -1.44
• 重原子数：
  12
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.89
• 拓扑面积：
  17.1
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为产物：
  描述：

  N-甲基吡咯烷酮 、 正溴丁烷 以 乙腈 为溶剂， 反应 3.0h， 以98.1%的产率得到1-butyl-1-methyl-2-oxopyrrolidinium bromide
  参考文献：
  名称：

  Probing HSA-ionic liquid interactions by spectroscopic and molecular docking methods

  摘要：

  Herein, we report the interaction of synthesized pyrrolidinium based ionic liquid, N-butyl-N-methyl-2-oxopyrrolidinium bromide (BMOP) with human serum albumin (HSA). The BMOP was characterized by using (1)H NMR, (13)C NMR and FT-IR techniques. The critical micelle concentration (cmc) of BMOP was confirmed by surface tension, conductivity and contact angle measurements. The interactions between HSA and BMOP were studied by steady-state and time-resolved fluorescence, UV-visible, FT-IR spectroscopic and molecular docking methods. The steady-state fluorescence spectra showed that BMOP quenched the fluorescence of HSA through combined quenching mechanism. Corresponding thermodynamic parameters viz. Gibbs free energy change (ΔG), entropy change (ΔS) and enthalpy change (ΔH) illustrated that the binding process was spontaneous and entropy driven. It is also suggested that hydrophobic forces play a key role in the binding of BMOP to HSA. In addition, the pyrene probe analysis again suggests the involvement of hydrophobic interaction in HSA-BMOP complex formation. Surface tension profile showed that the cmc value of BMOP in the presence of HSA is higher than the cmc value of pure BMOP. The FT-IR results show a conformational change in the secondary structure of HSA upon the addition of BMOP. The molecular docking result indicated that BMOP binds with HSA at hydrophobic pocket domain IIA with hydrophobic and hydrogen bond interactions in which hydrophobic interactions are dominating.

  DOI：

  10.1016/j.jphotobiol.2014.05.009

文献信息

• Spectroscopic and docking studies on the interaction between pyrrolidinium based ionic liquid and bovine serum albumin
  作者：Meena Kumari、Jitendra Kumar Maurya、Upendra Kumar Singh、Abbul Bashar Khan、Maroof Ali、Prashant Singh、Rajan Patel

  DOI：10.1016/j.saa.2014.01.012

  日期：2014.4

  The interaction of synthesized ionic liquid, 1-butyl-1-methyl-2-oxopyrrolidinium bromide (BMOP) and bovine serum albumin (BSA) was investigated using UV-Vis, FT-IR, steady state and time resolved fluorescence measurements and docking studies. Steady state spectra revealed that BMOP strongly quenched the intrinsic fluorescence of BSA through dynamic quenching mechanism. The corresponding thermodynamic parameters; Gibbs free energy change (AG), entropy change (Delta S) and enthalpy change (Delta H) showed that the binding process was spontaneous and entropy driven. It is also indicated that hydrophobic forces play a key role in the binding of BMOP to BSA. The synchronous fluorescence spectroscopy reveals that the conformation of BSA changed in the presence of BMOP. The shift in amide I band of FT-IR spectrum of BSA suggested unfolding of the protein secondary structure upon the addition of BMOP. In addition, the molecular modeling study of BSA-BMOP system shows that BMOP binds with BSA at the interface between two sub domains IIA and IIIA, which is located just above the entrance of the binding pocket of IIA through hydrophobic and hydrogen bond interactions in which hydrophobic interaction are dominated. (C) 2014 Elsevier B.V. All rights reserved.