Magnetic nanoparticle mediated enhancement of localized surface plasmon resonance for ultrasensitive bioanalytical assay in human blood plasma.
Magnetic nanoparticle mediated enhancement of localized surface plasmon resonance for ultrasensitive bioanalytical assay in human blood plasma.
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DOI:
10.1021/ac302422k
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发表时间:
2013-02-05
影响因子:
7.4
通讯作者:
Venkataramasubramani, Meenakshi
中科院分区:
文献类型:
--
作者:
Tang, Liang;Casas, Justin;Venkataramasubramani, Meenakshi
We demonstrate that Fe3O4 magnetic nanoparticle (MNP) can greatly enhance the localized surface plasmon resonance (LSPR) of metal nanoparticle. The high refractive index and molecular weight of the Fe3O4 MNPs make them a powerful enhancer for plasmonic response to biological binding events, thereby enabling a significant improvement in the sensitivity, reliability, dynamic range, and calibration linearity for LSPR assay of small molecules in trace amount. Rather than using fluorescence spectroscopy or magnetic resonance imaging, this study marks the first use of the label-free LSPR nanosensor for a disease biomarker in physiological solutions, providing a low cost, clinical-oriented detection. This facile and ultrasensitive nanosensor with extremely light, robust, and low-cost instrument is attractive for miniaturization on a lab-on-a-chip system to deliver point-of-care medical diagnostics. To further evaluate the practical application of Fe3O4 MNPs in the enhancement of LSPR assay, cardiac troponin I (cTnI) for myocardial infarction diagnosis was used as a model protein to be detected by a gold nanorod (GNR) bioprobe. MNP-captured cTnI molecules resulted in spectral responses up to 6 fold higher than direct cTnI adsorption on the GNR sensor. The detection limit (LOD) was lowered to ca. 30 pM for plasma samples which is 3 orders lower than comparable study. To the best of our knowledge, this marks the lowest LOD for a real plasma protein detection based on label-free LSPR shift without complicated instrumentation. The observed LSPR sensing enhancement by Fe3O4 MNPs is independent of nonspecific binding.
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