Suppr超能文献

胆碱氢氧化物负载磁性纳米粒子对细胞色素 c 过氧化物酶活性和构象稳定性的影响。

Impact of Choline Hydroxide-Supported Magnetic Nanoparticles on Peroxidase Activity and Conformational Stability of Cytochrome c.

机构信息

Department of Chemistry, University of Delhi, Delhi 110 007, India.

Department of Chemistry, Hansraj College, University of Delhi, Delhi 110007, India.

出版信息

ACS Appl Bio Mater. 2024 Feb 19;7(2):1135-1145. doi: 10.1021/acsabm.3c01052. Epub 2024 Jan 23.

Abstract

Nanotechnology has advanced significantly; however, little is known about the potential implications on human health-related issues, particularly blood carrying enzymes. Ionic liquids are also well-recognized for maintaining the structure and activity of enzymes. In this regard, we delineate a facile synthetic approach of preparation of FeO nanoparticles (NPs) as well as choline hydroxide [CH][OH] ionic liquid (IL)-supported FeO NPs (FeO-CHOH). This approach of combining magnetic nanoparticles (MNPs) with IL results in distinctive properties, which may offer enormous utility in the field of biomedical research due to the effortless separation of MNPs by an external magnetic field. Detailed characterization of MNPs including Fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD), Raman spectroscopy, transmission electron microscopy (TEM), and scanning electron microscopy (SEM) was carried out. The biomolecular interactions of FeO and FeO-CHOH NPs with cytochrome c (Cyt c) were studied in detail using various spectroscopic and microscopic techniques. From spectroscopic studies, it can be concluded that the secondary structure of Cyt c is more stable in the presence of FeO-CHOH NPs than FeO NPs. The binding constant of Cyt c in the presence of MNPs was also calculated using the Benesi-Hildebrand equation. Furthermore, dynamic light scattering (DLS), ζ-potential, and microscopic studies were performed to study the interaction of Cyt c with MNPs. These studies provided evidence favoring the formation of bionanoconjugates of Cyt c with MNPs. Moreover, the enzymatic activity of Cyt c increases in the presence of both MNPs. The peroxidase activity of Cyt c in MNPs explicitly elucidates that the enzyme is preserved for a long time in the presence of FeO-CHOH NPs. Later on, TEM and field emission scanning electron microscopy (FESEM) were also performed to gather more information regarding the morphology of Cyt c in the presence of MNPs.

摘要

纳米技术已经取得了显著的进展;然而,对于其可能对与人类健康相关的问题,特别是携带血液的酶,人们知之甚少。离子液体也因能够维持酶的结构和活性而得到广泛认可。在这方面,我们阐述了一种简便的制备方法,即用 FeO 纳米颗粒(NPs)和胆碱氢氧化物[CH][OH]离子液体(IL)来制备负载 FeO 的 NPs(FeO-CHOH)。这种将磁性纳米颗粒(MNPs)与 IL 结合的方法具有独特的性质,由于 MNPs 可以在外磁场的作用下轻易分离,因此可能在生物医学研究领域具有巨大的应用价值。我们对 MNPs 进行了详细的特性分析,包括傅里叶变换红外光谱(FTIR)、X 射线衍射(XRD)、拉曼光谱、透射电子显微镜(TEM)和扫描电子显微镜(SEM)。我们使用各种光谱和显微镜技术详细研究了 FeO 和 FeO-CHOH NPs 与细胞色素 c(Cyt c)的生物分子相互作用。从光谱研究可以得出结论,与 FeO NPs 相比,FeO-CHOH NPs 存在时 Cyt c 的二级结构更稳定。还使用 Benesi-Hildebrand 方程计算了 Cyt c 在 MNPs 存在下的结合常数。此外,还进行了动态光散射(DLS)、ζ-电势和显微镜研究,以研究 Cyt c 与 MNPs 的相互作用。这些研究提供了有利于 Cyt c 与 MNPs 形成生物纳米复合物的证据。此外,Cyt c 在两种 MNPs 存在下的酶活性均增加。Cyt c 在 MNPs 中的过氧化物酶活性明确表明,在 FeO-CHOH NPs 存在下,酶可以长时间保存。后来,还进行了 TEM 和场发射扫描电子显微镜(FESEM),以获取有关 Cyt c 在 MNPs 存在下形态的更多信息。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验