ArticleBioconjugate chemistry2012
Detection of MMP-2 and MMP-9 activity in vivo with a triple-helical peptide optical probe.
Article in Bioconjugate chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Article
- Applications of Matrix Metalloproteinase-9-Related Nanomedicines in Tumors and Vascular Diseases.Pharmaceutics · 2025Review
- Matrix Metalloproteinase-9: A Key Diagnostic Biomarker in Cancer Progression.Current drug targets · 2025Review
- Electrochemiluminescence biosensor for MMP-2 determination using CRISPR/Cas13a and EXPAR amplification: a novel approach for anti-aging research.Mikrochimica acta · 2024Article
- Early Expression of MMP-9 Predicts Recovery of Tibialis Anterior after Sciatic Nerve Crush Injury.Plastic and reconstructive surgery. Global open · 2022Article
- Gold nanoparticles conjugated with DNA aptamer for photoacoustic detection of human matrix metalloproteinase-9.Photoacoustics · 2022Article
- High-dose vitamin D metabolite delivery inhibits breast cancer metastasis.Bioengineering & translational medicine · 2022Article
- Research progress of near-infrared fluorescence probes based on indole heptamethine cyanine dyes in vivo and in vitro.BMC chemistry · 2020Review
- Assessing the range of enzymatic and oxidative tunability for biosensor design.Journal of materials chemistry. B · 2020Review
- Photoactive properties of supramolecular assembled short peptides.Chemical Society reviews · 2019Review
- Reducing off target viral delivery in ovarian cancer gene therapy using a protease-activated AAV2 vector platform.Journal of controlled release : official journal of the Controlled Release Society · 2019Article
- In Vivo Biosensing Using Resonance Energy Transfer.Biosensors · 2019Review
- Dissecting MMP PThe Journal of biological chemistry · 2018Article
- The Impact of Human Papilloma Viruses, Matrix Metallo-Proteinases and HIV Protease Inhibitors on the Onset and Progression of Uterine Cervix Epithelial Tumors: A Review of Preclinical and Clinical Studies.International journal of molecular sciences · 2018Review
- Development of a Protease Biosensor Based on a Dimerization-Dependent Red Fluorescent Protein.ACS chemical biology · 2018Article
- A reduced graphene oxide-based fluorescence resonance energy transfer sensor for highly sensitive detection of matrix metalloproteinase 2.International journal of nanomedicine · 2016Article
- Long-wavelength analyte-sensitive luminescent probes and optical (bio)sensors.Methods and applications in fluorescence · 2015Article
- MMP-2/9-Specific Activatable Lifetime Imaging Agent.Sensors (Basel, Switzerland) · 2015Article
- New tools for the quantitative assessment of prodrug delivery and neurotoxicity.Neurotoxicology · 2015Article
- Basis for substrate recognition and distinction by matrix metalloproteinases.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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7 authors.
Funding
Abstract
We report a novel activatable NIR fluorescent probe for in vivo detection of cancer-related matrix metalloproteinase (MMP) activity. The probe is based on a triple-helical peptide substrate (THP) with high specificity for MMP-2 and MMP-9 relative to other members of the MMP family. MMP-2 and MMP-9 (also known as gelatinases) are specifically associated with cancer cell invasion and cancer-related angiogenesis. At the center of each 5 kDa peptide strand is a gelatinase sensitive sequence flanked by 2 Lys residues conjugated with NIR fluorescent dyes. Upon self-assembly of the triple-helical structure, the 3 peptide chains intertwine, bringing the fluorophores into close proximity and reducing fluorescence via quenching. Upon enzymatic cleavage of the triple-helical peptide, 6 labeled peptide chains are released, resulting in an amplified fluorescent signal. The fluorescence yield of the probe increases 3.8-fold upon activation. Kinetic analysis showed a rate of LS276-THP hydrolysis by MMP-2 (k(cat)/K(M) = 30,000 s(-1) M(-1)) similar to that of MMP-2 catalysis of an analogous fluorogenic THP. Administration of LS276-THP to mice bearing a human fibrosarcoma xenografted tumor resulted in a tumor fluorescence signal more than 5-fold greater than that of muscle. This signal enhancement was reduced by treatment with the MMP inhibitor Ilomostat, indicating that the observed tumor fluorescence was indeed enzyme mediated. These results are the first to demonstrate that triple-helical peptides are suitable for highly specific in vivo detection of tumor-related MMP-2 and MMP-9 activity.
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