Construction of PEGylated Fe<sub>۳</sub>O<sub>۴</sub>@SiO<sub>۲</sub> Functionalized by Hydrazine Toward Solid Phase Extraction, Enrichment, and Determination of IgG Glycoprotein

سال انتشار: 1405
نوع سند: مقاله ژورنالی
زبان: انگلیسی
مشاهده: 28

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شناسه ملی سند علمی:

JR_ANALCH-13-3_005

تاریخ نمایه سازی: 16 تیر 1405

چکیده مقاله:

Immunoglobulin G (IgG) is the most abundant serum antibody and a key biomarker in diagnostics, yet its accurate determination remains challenging due to its structural complexity and the interference of diverse biomolecules in biological matrices. Reliable detection and enrichment of IgG are therefore essential for advancing clinical diagnostics, therapeutic monitoring, and biomedical research. In this study, we report the construction of core-shell magnetic Fe۳O۴@SiO۲ nanoparticles functionalized with PEGylated hydrazine groups (Fe۳O۴@SiO۲@P(G-PEG-G-co-NH۲-NH۲)), designated as Magnetic PEG-Hydrazine Nanoadsorbent (M-PEG-HZNA), and evaluate their potential for the solid-phase extraction, enrichment, and determination of IgG glycoprotein. The resulting core-shell nanomaterial exhibited a uniform size distribution (average diameter ~۶۲ nm) and a high density of accessible functional groups, enabling selective interactions with glycoproteins. The morphology, structure, and surface chemistry of the nanoadsorbent were systematically characterized employing TEM, FE-SEM, TGA, DLS, XRD, VSM, and FT-IR spectroscopy, confirming its successful synthesis and stability. To optimize adsorption performance, key operational parameters, including solution pH, incubation time, and adsorbent dosage, were systematically investigated, with maximum adsorption achieved at pH ۹.۳. Under optimized conditions, M-PEG-HZNA exhibited a strong enrichment capacity for IgG. Adsorption equilibrium studies indicated that the binding process was well described by the Langmuir isotherm model, with a maximal adsorption capacity of ۱۲۹.۸ mg/g. Importantly, M-PEG-HZNA not only enabled efficient capture and enrichment of IgG but also demonstrated its potential as a robust platform for glycoprotein isolation and analytical applications in biomedical and clinical research.

نویسندگان

Sanaz Mansouri Gharaghoushi

aDepartment of Chemistry, Islamic Azad University, Central Tehran Branch, Iran

Mahshid Nikpour Nezhati

Department of Chemistry, Islamic Azad University, Central Tehran Branch, Iran

Habibollah Baharvand

bFaculty of Polymer Science, Iran Polymer and Petrochemical Institute, Tehran, Iran

Taher Mohammadian

Department of Microbiology, Shahr-e-Qods-Branch, Islamic Azad University, Tehran, Iran

Homayon Ahmad Panahi

Department of Chemistry, Islamic Azad University, Central Tehran Branch, Iran