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Effect of N-Butyl-N-Methyl-Morpholinium Bromide Ionic Liquid on the Conformation Stability of Human Serum Albumin

机译:N-丁基-N-甲基溴化溴离子液体对人血清白蛋白构象稳定性的影响

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摘要

The present work reports the interaction of morpholinium based ionic liquid with the transporter protein, human serum album (HSA). The ionic liquids with morpholinium cationic groups are reported to be comparatively less toxic than other cationic groups of the ionic liquids such as imidazolium, pyridinium, piperidinium, pyrrolidinium etc. This work highlight the effect of N-butyl-N-methyl-morpholinium bromide, [Mor1,4] [Br] ionic liquid on the structural stability of HSA. The effect was analyzed by using fluorescence, time resolved fluorescence, UVvisible, CD spectroscopic techniques and molecular docking method. The results show that [Mor1,4][Br] binds with HSA through weak interactions in which hydrogen bonding and van der Waals forces play major role. [Mor1,4][Br] has a binding site on HSA and binds in the hydrophobic pocket of subdomain IIA of HSA. It was observed that [Mor1,4][Br] retain native conformation of HSA upto certain concentration range. This study endows new insight for designing of such type of nontoxic ILs that augments their protein stabilizing nature.
机译:目前的工作报告了形态基离子液体与转运蛋白人血清专辑(HSA)的相互作用。据报道,带有形态阳离子基的离子液体比其他离子液体的阳离子基团(如咪唑啉,吡啶丁胺,哌啶,吡咯啶等)的毒性相对较小。这种工作突出了N-丁基-N-甲基 - 甲基 - 甲基酚基的效果, [MOR1,4] [Br]离子液体对HSA的结构稳定性。通过使用荧光,时间分辨的荧光,紫外线,CD光谱技术和分子对接方法来分析该效果。结果表明,[MOR1,4] [BR]通过弱相互作用与HSA结合,其中氢键和范德华力作用起着主要作用。 [MOR1,4] [Br]在HSA上具有结合位点,并在HSA亚域IIA的疏水口袋中结合。据观察,[MOR1,4] [BR]将HSA的天然构象保持在一定浓度范围内。这项研究赋予了设计这种类型的无毒IL的新见解,从而增强其蛋白质稳定性。

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