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Enzyme-Anchored Signal Amplification: A Dual-Modal Probe for Precise Imaging of Orthotopic Lung Cancer via
Jiani Wang1,2, Sha Li1,2, Maosong Qiu1,2
1State Key Laboratory of Magnetic Resonance Spectroscopy and Imaging, National Center for Magnetic Resonance in Wuhan, Wuhan Institute of Physics and Mathematics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, P. R. China.
None:
Hypoxia-induced overexpression of nitroreductase is a hallmark of aggressive lung tumors, yet conventional diagnostic probes often suffer from rapid diffusion and low signal retention, compromising diagnostic precision. To overcome these hurdles, we developed NO2-Cy-cRGD-Gd, an NTR-responsive dual-mode fluorescence (FL) and 1H magnetic resonance imaging probe featuring an innovative in situ protein-anchoring mechanism. Upon αvβ3 integrin-mediated internalization, NTR-triggered reduction generates a reactive quinone methide intermediate that covalently binds to intracellular proteins, effectively "locking" the diagnostic signal within the tumor. This immobilization strategy simultaneously activates a 40.9-fold near-infrared FL enhancement and a 104.2% increase in longitudinal relaxivity (r1) while ensuring prolonged intratumoral retention. Validated in both subcutaneous and orthotopic lung cancer models, the probe demonstrated exceptional specificity and clearly delineated the tumor boundaries. By integrating targeted delivery with enzyme-activated covalent anchoring, this work provides a robust strategy for high-contrast, dual-mode imaging and precise surgical navigation in hypoxic malignancies.
