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Purpose  Since matrix metalloproteinase-2 (MMP-2) is an important marker of tumor malignancy, we developed an original drug design strategy, MMP-2 activity dependent anchoring probes (MDAP), for use in MMP-2 activity imaging, and evaluated the usefulness of this probe in  in vitro  and  in vivo  experiments.    Methods  We designed and synthesized MDAP 1000 , MDAP 3000 , and MDAP 5000 , which consist of 4 independent moieties: RI unit ( 111 In hydrophilic chelate), MMP-2 substrate unit (short peptide), anchoring unit (alkyl chain), and anchoring inhibition unit (polyethylene glycol (PEGn; where n represents the approximate molecular weight, n = 1000, 3000, and 5000). Probe cleavage was evaluated by chromatography after MMP-2 treatment. Cellular uptake of the probes was then measured. Radioactivity accumulation in tumor xenografts was evaluated after intravenous injection of the probes, and probe cleavage was evaluated in tumor homogenates.    Results  MDAP 1000 , MDAP 3000 , and MDAP 5000  were cleaved by MMP-2 in a concentration-dependent manner. MDAP 3000  pretreated with MMP-2 showed higher accumulation in tumor cells, and was completely blocked by additional treatment with an MMP inhibitor. MDAP 3000  exhibited rapid blood clearance and a high tumor accumulation after intravenous injection in a rodent model. Furthermore, pharmacokinetic analysis revealed that MDAP 3000  exhibited a considerably slow washout rate from tumors to blood. A certain fraction of cleaved MDAP 3000  existed in tumor xenografts  in vivo .    Conclusions  The results indicate the possible usefulness of our MDAP strategy for tumor imaging.

Investigation of a MMP-2 Activity-Dependent Anchoring Probe for Nuclear Imaging of Cancer