Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 23, Issue 3, Pages -Publisher
MDPI
DOI: 10.3390/ijms23031605
Keywords
activatable peptides; fluorescent imaging; proteases; MMP2; cancer cells
Funding
- National Research Foundation of Korea (NRF) - Korean government (MSIT) [2019R1A2C2004858]
- NRF - Ministry of Education [2020R1A6A1A06046728]
- KIST Institutional Program [2Z06270-20-137]
- Korea Environment Industry and Technology Institute (KEITI) - Korea Ministry of Environment (MOE) [2020003030007]
- National Research Foundation of Korea [2019R1A2C2004858, 2020R1A6A1A06046728] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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In this study, a cell-based fluorescent peptide method was demonstrated for monitoring protease activity. By utilizing MMP2 secreted by living cancer cells, the activatable peptide is able to be delivered intracellularly and exhibit fluorescence response. This approach is expected to enable rapid visualization of protease activity in living cells.
Activity-based monitoring of cell-secreted proteases has gained significant interest due to the implication of these substances in diverse cellular functions. Here, we demonstrated a cell-based method of monitoring protease activity using fluorescent cell-permeable peptides. The activatable peptide consists of anionic (EEEE), cleavable, and cationic sequences (RRRR) that enable intracellular delivery by matrix metalloproteinase-2 (MMP2), which is secreted by living cancer cells. Compared to HT-29 cells (MMP2-negative), HT-1080 cells (MMP2-positive) showed a strong fluorescence response to the short fluorescent peptide via cell-secreted protease activation. Our approach is expected to find applications for the rapid visualization of protease activity in living cells.
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