Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/82872
Title: Sensitive surface enhanced Raman scattering multiplexed detection of matrix metalloproteinase 2 and 7 cancer markers
Authors: Gong, Tianxun
Kong, Kien Voon
Goh, Douglas
Olivo, Malini
Yong, Ken-Tye
Keywords: Medical optics
Issue Date: 2015
Source: Gong, T., Kong, K. V., Goh, D., Olivo, M., & Yong, K.-T. (2015). Sensitive surface enhanced Raman scattering multiplexed detection of matrix metalloproteinase 2 and 7 cancer markers. Biomedical Optics Express, 6(6), 2076-2087.
Series/Report no.: Biomedical Optics Express
Abstract: A surface enhanced Raman spectroscopy (SERS) based platform was developed for sensitive multiplexed detection of matrix metalloproteinases (MMP) (MMP-2 and MMP-7) with low limit of detection and high specificity. Detection is based on the virtue of enzymatic reaction where a peptide can be cleaved only by its corresponding enzyme. The platform comprises two components, a specialized SERS-based bimetallic-film-over-nanosphere (BMFON) substrate and gold nanoparticles (AuNPs). The two components were functionalized such that binding between the two would occur through biotin-avidin-biotin complexation. Binding is hindered by MMP peptide chains conjugated onto the surfaces of the substrate and AuNPs, and can be removed only by cleaving the peptide chains with corresponding enzymes. Since AuNP binding sites become free after the peptides are cleaved, the number of binding sites for AuNPs onto the substrate would increase. By tagging the AuNPs, concentrations of MMP-specific enzymes can be quantified through examining intensities of signature SERS peaks of the tags. This cleave-and-bind mechanism was first validated by individual detection and quantification of MMP-2 and MMP-7. The platform was demonstrated to be able to sensitively detect concentrations of specific enzymes ranging from 1 ng/mL to 40 μg/mL, with close correlation between SERS intensity and concentrations. Finally, the multiplexed detection of MMP-2 and MMP-7 was demonstrated. The multiplexity of this platform provides a robust way to analyze diseases associated with MMP-2 and MMP-7 enzymes. Our work can be further developed as a clinical diagnostic tool to detect other MMP proteinase in bio-fluids samples, widening the number of biomarkers needed to characterize diseases better
URI: https://hdl.handle.net/10356/82872
http://hdl.handle.net/10220/40384
ISSN: 2156-7085
DOI: 10.1364/BOE.6.002076
Rights: © 2015 Optical Society of America. This is the author created version of a work that has been peer reviewed and accepted for publication by Biomedical Optics Express, Optical Society of America. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1364/BOE.6.002076].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:EEE Journal Articles

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