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Related Concept Videos

Enzyme-Linked Immunosorbent Assay01:33

Enzyme-Linked Immunosorbent Assay

In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen.  Enzyme-substrate reaction allows the antigen to be visualized or quantified.
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Related Experiment Video

Updated: Jun 11, 2026

An In Vitro Single-Molecule Imaging Assay for the Analysis of Cap-Dependent Translation Kinetics
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In Situ Enzyme Activity Analysis in Single Living Cells Based on the EISA Reaction and Rotation or Translation

Yichao Xiao1, Kun Zang1, Xintong Lu1

  • 1State Key Laboratory of Synergistic Chem-Bio Synthesis, School of Chemistry and Chemical Engineering, Shanghai Jiao Tong University, Shanghai 200240, P. R. China.

Analytical Chemistry
|June 10, 2026
PubMed
Summary
This summary is machine-generated.

A new spectroscopy method quantifies enzyme activity in single cells. This technique uses enzyme-instructed self-assembly and single-particle rotation or translation correlation spectroscopy (RTCS) to measure caspase-3 activity, aiding drug discovery.

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Area of Science:

  • Biophysics
  • Cellular Biology
  • Spectroscopy

Background:

  • Enzymes are vital for cellular functions.
  • Limited in situ methods exist for quantitative single-cell enzyme activity analysis.
  • Existing imaging methods lack quantitative precision.

Purpose of the Study:

  • To develop a novel single-particle spectroscopy method for quantifying enzyme activity within single living cells.
  • To establish an in situ quantitative analysis method for caspase-3 activity.
  • To demonstrate the method's potential for studying enzyme functions and inhibitor screening.

Main Methods:

  • Enzyme-instructed self-assembly (EISA) reaction combined with single-particle rotation or translation correlation spectroscopy (RTCS).
  • Utilized fluorescent peptide nanorods self-assembled via caspase-3-induced EISA.
  • Measured RTCS curves to extract rotational and translational diffusion times.

Main Results:

  • Established a quantitative method for caspase-3 activity based on ratiometric diffusion time.
  • Determined the distribution of caspase-3 activity within single cells.
  • Successfully measured the inhibition effect of an inhibitor on caspase-3 activity.

Conclusions:

  • The developed single-particle spectroscopy method enables quantitative measurement of caspase-3 activity in single cells.
  • This technique shows significant potential for studying enzymatic functions in native biological contexts.
  • The method is valuable for high-throughput inhibitor screening and understanding enzyme kinetics at the single-cell level.