ArticleChemistry & biology2011
Directed evolution of protease beacons that enable sensitive detection of endogenous MT1-MMP activity in tumor cell lines.
Article in Chemistry & biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Analysis of Matrix Metalloproteinase Activity and Inhibition in Cancer Spheroids.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Application of FRET Biosensors in Mechanobiology and Mechanopharmacological Screening.Frontiers in bioengineering and biotechnology · 2020Review
- Characterization and regulation of MT1-MMP cell surface-associated activity.Chemical biology & drug design · 2019Article
- Intracellular FRET-based Screen for Redesigning the Specificity of Secreted Proteases.ACS chemical biology · 2016Article
- High-Throughput Multiplexed Peptide-Centric Profiling Illustrates Both Substrate Cleavage Redundancy and Specificity in the MMP Family.Chemistry & biology · 2015Article
- Article
- Article
- Chemical biology for understanding matrix metalloproteinase function.Chembiochem : a European journal of chemical biology · 2012Review
- Identification of protease exosite-interacting peptides that enhance substrate cleavage kinetics.Biological chemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Directed evolution was applied to identify peptide substrates with enhanced hydrolysis rates by MT1-MMP suitable for protease beacon development. Screening of a random pentapeptide library, using two-color CLiPS, yielded several substrates identical to motifs in distinct collagens that shared the consensus sequence P-x-G↓L. To identify substrates with enhanced cleavage rates, a second-generation decapeptide library incorporating the consensus was screened under stringent conditions, which resulted in a MxPLG↓(M)/(L)M(G)/(A)R consensus motif. These substrates are hydrolyzed by human-MT1-MMP up to six times faster than reported peptide substrates and are stable in plasma. Finally, incubation of soluble protease beacons incorporating the optimized substrates, but not previous substrates, enabled direct detection of endogenous MT1-MMP activity of human-fibrosarcoma (HT-1080) cells. Extended substrate libraries coupled with CLiPS should be useful to generate more effective activity probes for a variety of proteolytic enzymes.
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