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Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

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Conjugated polyelectrolyte supported bead based assays for phospholipase A2 activity.

Sireesha Chemburu¹, Eunkyung Ji, Yosune Casana

¹Department of Chemical and Nuclear Engineering, University of New Mexico, Albuquerque, New Mexico 87131, USA.

The Journal of Physical Chemistry. B

|September 24, 2008

Summary

A novel fluorescence assay using lipobeads detects human serum phospholipase A2 (PLA2) activity. This sensitive method offers nanomolar detection, aiding in understanding PLA2

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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

Area of Science:

Biochemistry
Analytical Chemistry
Biotechnology

Background:

Phospholipase A2 (PLA2) enzymes play crucial roles in various physiological and pathological processes.
Accurate and sensitive detection of PLA2 activity is essential for biological research and clinical diagnostics.
Existing assays may have limitations in sensitivity, specificity, or ease of use.

Purpose of the Study:

To develop a novel, sensitive, and robust fluorescence-based assay for quantifying human serum-derived phospholipase A2 (PLA2) activity.
To utilize engineered "lipobeads" as a sensor platform for PLA2 detection.
To explore different quenching mechanisms for enhanced signal transduction.

Main Methods:

Development of silica microspheres coated with cationic conjugated polyelectrolytes.
Overcoating of polymer-coated beads with anionic phospholipid (1,2-dimyristoyl-sn-glycero-3-[phospho-rac-(1-glycerol)) (DMPG) to create "lipobeads".
Utilizing external electron transfer quenchers (e.g., AQS) or lipid-based quenchers to modulate polymer fluorescence upon PLA2 digestion.
Detection of fluorescence changes using a multiwell plate reader and flow cytometry.

Main Results:

The developed assay demonstrates high sensitivity for PLA2 activity, with EC50 values in the nanomolar range.
Two distinct fluorescence quenching strategies were successfully implemented, both correlating with PLA2 digestion.
The assay is adaptable for both plate-based and flow cytometry detection methods.
The lipobeads effectively serve as both substrate and sensor components.

Conclusions:

A sensitive and versatile fluorescence-based assay for human serum PLA2 activity has been successfully developed.
The "lipobead" platform offers a promising approach for enzyme activity detection.
The assay's sensitivity and adaptability make it suitable for various research and diagnostic applications.