20 February 2018 Dual-radiolabeled nanoparticle probes for depth-independent in vivo imaging of enzyme activation
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Quantitative and noninvasive measurement of protease activities has remained an imaging challenge in deep tissues such as the lungs. Here, we designed a dual-radiolabeled probe for reporting the activities of proteases such as matrix metalloproteinases (MMPs) with multispectral single photon emission computed tomography (SPECT) imaging. A gold nanoparticle (NP) was radiolabeled with 125I and 111In and functionalized with an MMP9-cleavable peptide to form a multispectral SPECT imaging contrast agent. In another design, incorporation of 199Au radionuclide into the metal crystal structure of gold NPs provided a superior and stable reference signal in lungs, and 111In was linked to the NP surface via a protease-cleavable substrate, which can serve as an enzyme activity reporter. This work reveals strategies to correlate protease activities with diverse pathologies in a tissue-depth independent manner.
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Kvar C. L. Black, Mingzhou Zhou, Pinaki Sarder, Maryna Kuchuk, Amal Y. Al-Yasiri, Sean P. Gunsten, Kexian Liang, Heather M. Hennkens, Walter J. Akers, Richard Laforest, Steven L. Brody, Cathy S. Cutler, Samuel Achilefu, "Dual-radiolabeled nanoparticle probes for depth-independent in vivo imaging of enzyme activation", Proc. SPIE 10508, Reporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications X, 1050805 (20 February 2018); doi: 10.1117/12.2301033; https://doi.org/10.1117/12.2301033

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