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Recently, the research team led by Tian Changlin from the Center for High Magnetic Field Research at the Chinese Academy of Sciences published an article titled "EPR-based in situ enzymatic activity detection of endogenous caspase-3 in apoptosis cell lysates" in Chemical Communications. The team established an enzyme activity analysis method based on electron paramagnetic resonance (EPR) technology using peptide probes and BeaverBeads® Streptavidin to quickly detect the activity of caspase-3 in cells.
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Cell apoptosis, also known as programmed cell death, is a highly regulated and evolutionarily conserved process. Dysfunction of cell apoptosis can lead to various diseases. Therefore, the development of detection and research methods for cell apoptosis is important for clinical diagnosis and treatment research.
Caspase family plays a crucial role in cell apoptosis. Among the family, caspase-3 is the most frequently activated protease in early apoptosis and is considered the most important biomarker in apoptosis-related research. Therefore, the detection of caspase-3 activity has become not only an important topic in the diagnosis of cell apoptosis but also an important topic in evaluating treatment effectiveness.
Electron paramagnetic resonance (EPR) spectroscopy is a powerful method for detecting and studying paramagnetic species in biological and chemical systems. In recent years, EPR has become a suitable tool for analysis and research due to its high sensitivity.
In this study, the researchers creatively invented an enzyme activity analysis method based on EPR technology that can reliably and quickly detect the activity of caspase-3 in the process of cell apoptosis. They first synthesized a peptide segment (DEVD) that can specifically recognize caspase-3 and then biotinylated it. They labeled the peptide segment with a nitroxide free radical (MTSL) that can be detected by EPR. The spin-labeled peptide probe was combined with BeaverBeads® Streptavidin (2.8μm) (MBs) to form a "nitroxide-peptide-magnetic bead" sandwich complex probe structure. The prepared probe was incubated with the sample, and the activity of caspase-3 was detected by EPR signal. In the absence of caspase-3, the supernatant did not show an EPR signal after magnetic separation (EPR "closed"). However, when caspase-3 was present, caspase-3 specifically degraded DEVD, and the terminal nitroxide part was released into the solution, which showed an EPR signal (EPR "opened"). Also we also have peptide prdoucts of the cu cosmetics type.
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