REDUCING NON-SPECIFIC ADSORPTION OF PROTEINS VIA THE HPG MODIFICATION ON THE SURFACE OF MAGNETIC NANOPARTICLES

IF 0.5 4区 化学 Q4 CHEMISTRY, MULTIDISCIPLINARY Quimica Nova Pub Date : 2023-03-03 DOI:10.21577/0100-4042.20170950
Mengbo Zhou, Chunyu Sun, Hong Zhao
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Abstract

Reducing non-specific adsorption of proteins on the surface of magnetic nanoparticles (MNPs) is becoming increasingly important. In this paper, we proposed a novel surface modification procedure by grafting hyperbranched polyglycerol (HPG) onto the surface of MNPs (Fe3O4@SiO2@MAA), in which lots of hydroxyl groups from HPG not only provide the hydrates sheath to prevent non-specific adsorption of proteins, but also react with succinic anhydride to generate carboxyl groups that serve as active sites to specifically bind proteins. The protein adsorption experiments showed that the non-specific adsorption (0.07 μg mg-1) was reduced to 4.58% of that before modification. It also showed that the antigen binding capacity was 9.7 times higher than the original when detecting cardiac troponin I (cTnI) in human plasma samples, which indicated that the final synthesized MNPs had great application prospects in bio-separation and bioanalysis.
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通过HPG修饰磁性纳米颗粒表面减少蛋白质的非特异性吸附
减少磁性纳米颗粒(MNPs)表面蛋白质的非特异性吸附变得越来越重要。在本文中,我们提出了一种新的表面修饰方法,将超支化聚甘油(hyperbranched polyglycerol, HPG)接枝到MNPs (Fe3O4@SiO2@MAA)表面,其中HPG的大量羟基不仅提供水合物鞘以防止蛋白质的非特异性吸附,而且与琥珀酸酐反应生成羧基,作为特异性结合蛋白质的活性位点。蛋白质吸附实验表明,非特异性吸附量(0.07 μg -1)降至修饰前的4.58%。在检测人血浆样品中的心肌肌钙蛋白I (cTnI)时,其抗原结合能力比原MNPs提高了9.7倍,表明最终合成的MNPs在生物分离和生物分析方面具有很大的应用前景。
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来源期刊
Quimica Nova
Quimica Nova 化学-化学综合
CiteScore
1.60
自引率
12.50%
发文量
72
审稿时长
2-4 weeks
期刊介绍: Química Nova publishes in portuguese, spanish and english, original research articles, revisions, technical notes and articles about education in chemistry. All the manuscripts submitted to QN are evaluated by, at least, two reviewers (from Brazil and abroad) of recognized expertise in the field of chemistry involved in the manuscript. The Editorial Council can be eventually asked to review manuscripts. Editors are responsible for the final edition of QN.
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