探讨表面活性剂对二氧化锰纳米颗粒与生物分子相互作用的影响。

IF 2.7 3区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Shagufta Khan, Prairna Balyan, Ahmad Ali, Shweta Sharma, Shilpee Sachar
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引用次数: 0

摘要

利用荧光(稳态、同步和三维)、紫外可见、共振光散射(RLS)、动态光散射(DLS)和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)研究了二氧化锰纳米颗粒(MnO2 NPs)与重要生物分子脱氧核糖核酸(DNA)和血清白蛋白(BSA)与不同表面活性剂的相互作用。测定了血清白蛋白酯酶活性与MnO2 NPs和表面活性剂的关系。采用DPPH法对NPs的抗氧化能力进行了评价。凝胶电泳分析了MnO2 NPs和表面活性剂对DNA的影响。CTAB、Tween 20、DTAB和Tween 80的存在增强了纳米颗粒与蛋白质的结合。基于Tween 20的纳米颗粒体系具有长期稳定性和生物相容性。MnO2 NPs单独存在以及与Tween 20一起存在时,BSA荧光发射猝灭,表明纳米颗粒与蛋白质的关联更强。在Tween 20的作用下,酯酶活性(BSA)明显增强。此外,Tween 20存在时自由基清除能力最强。蛋白质- nps结合的焓和熵评价显示范德瓦尔斯相互作用和氢键为主。同步荧光分析强调了色氨酸(Trp)参与MnO2 nps -蛋白相互作用。研究了表面活性剂对MnO2 NPs与必需生物分子结合的影响。研究结果可用于设计长期应用的生物相容性二氧化锰配方。由Ramaswamy H. Sarma传达。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Exploring the effect of surfactants on the interactions of manganese dioxide nanoparticles with biomolecules.

Interactions of manganese dioxide nanoparticles (MnO2 NPs) with vital biomolecules namely deoxyribonucleic acid (DNA) and serum albumin (BSA) have been studied in association with different surfactants by using fluorescence (steady state, synchronous and 3D), UV-visible, resonance light scattering (RLS), dynamic light scattering (DLS), and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The esterase activity of serum albumin was tested in associations with MnO2 NPs and surfactants. The antioxidant potential of prepared NPs was also evaluated (DPPH method). Gel electrophoresis was carried out to analyze the effect of MnO2 NPs and surfactants on DNA. Presence of CTAB, Tween 20, DTAB and Tween 80 enhanced nanoparticle-protein binding. Tween 20 based nanoparticle systems showed long-term stability and biocompatibility. The quenching of BSA fluorescence emission in presence of MnO2 NPs alone and along with Tween 20 revealed stronger association of nanoparticles with proteins. Enhancement in the esterase activity (BSA) was observed in the presence of Tween 20. Furthermore, radical scavenging activity showed highest antioxidant potential in presence of Tween 20. The enthalpy and entropy assessment for protein-NPs association showed the predominance of Vander Waals interactions and hydrogen bonding. The synchronous fluorescence analysis highlighted the involvement of tryptophan (Trp) in the MnO2 NPs-protein interactions. The study evaluates the influence of surfactant on the associations of MnO2 NPs with the essential biomolecules. The findings can be crucially utilized in designing biocompatible MnO2 formulations for long term applications.Communicated by Ramaswamy H. Sarma.

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来源期刊
Journal of Biomolecular Structure & Dynamics
Journal of Biomolecular Structure & Dynamics 生物-生化与分子生物学
CiteScore
8.90
自引率
9.10%
发文量
597
审稿时长
2 months
期刊介绍: The Journal of Biomolecular Structure and Dynamics welcomes manuscripts on biological structure, dynamics, interactions and expression. The Journal is one of the leading publications in high end computational science, atomic structural biology, bioinformatics, virtual drug design, genomics and biological networks.
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