Probing the conformational changes and peroxidase-like activity of cytochrome c upon interaction with iron nanoparticles

被引：41

作者：

Azad, Vida Jafari ^{[1
]}

Kasravi, Shahab ^{[2
]}

Zeinabad, Hojjat Alizadeh ^{[3
]}

Aval, Mehri Memar Bashi ^{[1
]}

Saboury, Ali Akbar ^{[4
]}

Rahimi, Arash ^{[5
]}

Falahati, Mojtaba ^{[1
]}

机构：

[1] Islamic Azad Univ IAUPS, Fac Adv Sci & Technol, Pharmaceut Sci Branch, Dept Nanotechnol, Tehran, Iran

[2] Islamic Azad Univ, Tehran Med Sci Branch, Dept Biol, Tehran, Iran

[3] Inst Res Fundamental Sci IPM, Brain Engn Res Ctr, POB 19395-5746, Tehran, Iran

[4] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran

[5] Islamic Azad Univ, Fac Basic Sci, Sci & Res Branch, Dept Biophys, Tehran, Iran

来源：

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS | 2017年 / 35卷 / 12期

关键词：

protein; conformational change; nanoparticle; activity; secondary structure; OXIDE NANOPARTICLES; SERUM-ALBUMIN; MRI CONTRAST; NANOMATERIALS; CYTOTOXICITY; APOPTOSIS; BINDING;

D O I：

10.1080/07391102.2016.1222972

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Herein, the interaction of iron nanoparticle (Fe-NP) with cytochrome c (Cyt c) was investigated, and a range of techniques such as dynamic light scattering (DLS), zeta potential measurements, static and synchronous fluorescence spectroscopy, near and far circular dichroism (CD) spectroscopy, and ultraviolet-visible (UV-vis) spectroscopy were used to analyze the interaction between Cyt c and Fe-NP. DLS and zeta potential measurements showed that the values of hydrodynamic radius and charge distribution of Fe-NP are 83.95 +/- 3.7nm and 4.5 +/-.8mV, respectively. The fluorescence spectroscopy results demonstrated that the binding of Fe-NP with Cyt c is mediated by hydrogen bonds and van der Waals interactions. Also Fe-NP induced conformational changes in Cyt c and reduced the melting temperature value of Cyt c from 79.18 to 71.33 degrees C. CD experiments of interaction between Fe-NP and Cyt c revealed that the secondary structure of Cyt c with the dominant -helix structures remained unchanged whereas the tertiary structure and heme position of Cyt c are subjected to remarkable changes. Absorption spectroscopy at 695nm revealed that Fe-NP considerably disrupt the Fe...S(Met80) bond. In addition, the UV-vis experiment showed the peroxidase-like activity of Cyt c upon interaction with Fe-NP. Hence, the data indicate the Fe-NP results in unfolding of Cyt c and subsequent peroxidase-like activity of denatured species. It was concluded that a comprehensive study of the interaction of Fe-NP with biological system is a crucial step for their potential application as intracellular delivery carriers and medicinal agents.

引用

页码：2565 / 2577

页数：13

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