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Immunoprecipitation

Immunoprecipitation

Immunoprecipitation, or IP, is a widely used technique that employs protein-antibody interactions to isolate proteins or protein complexes in their native state for studying protein-protein interactions, quaternary structures, or supramolecular complexes. Various modifications of the technique, including chromatin IP, cross-linking IP, and fluorescence IP, are commonly used.
Chromatin Immunoprecipitation
Chromatin immunoprecipitation, also known as ChIP, is used to study protein-DNA or...

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Related Experiment Video

Updated: Nov 5, 2025

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

Published on: September 14, 2018

Stable and Highly Efficient Antibody-Nanoparticles Conjugation.

Mahnaz Maddahfar^1,2, Shihui Wen¹, Seyed Mostafa Hosseinpour Mashkani¹

¹Institute for Biomedical Materials and Devices (IBMD), School of Mathematical and Physical Sciences, Faculty of Science, University of Technology Sydney, Sydney, New South Wales 2007, Australia.

Bioconjugate Chemistry

|May 20, 2021

Summary

This summary is machine-generated.

Optimizing polymer chain length is key for stable, antibody-conjugated nanoparticles. The study found 13 OEGMEA units balance nanoparticle stability and antibody binding for bio-nanoconjugate applications.

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Last Updated: Nov 5, 2025

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Area of Science:

Bioconjugation Chemistry
Materials Science
Nanotechnology

Background:

Functional ligands and polymers are crucial for creating target-specific bio-nanoconjugates.
Polyethylene glycol (PEG)-based polymers are widely used to modify nanoparticle properties.

Purpose of the Study:

To systematically investigate the impact of poly(oligo (ethylene glycol) methyl ether acrylate) (POEGMEA) chain length on nanoparticle colloidal stability and antibody conjugation efficiency.
To identify an optimal POEGMEA chain length for developing stable and bioactive nanoconjugates.

Main Methods:

Synthesis of diblock copolymers using Reversible Addition-Fragmentation Chain Transfer (RAFT) polymerization.
Incorporation of varying lengths of OEGMEA units (6, 13, 35, 55) with a constant number of monoacryloxyethyl phosphate (MAEP) units (7).
Characterization of nanoparticle stability and antibody conjugation efficiency, including flow cytometry assays.

Main Results:

Short POEGMEA chains resulted in poor nanoparticle stabilization.
Long POEGMEA chains hindered antibody conjugation due to inaccessible carboxylic groups.
The polymer with 13 OEGMEA units achieved the highest antibody binding (64%), with efficiency decreasing for longer chains (50% for 35 units, 0% for 55 units).
Approximately 9% of conjugated antibodies retained activity for B220 biomarker recognition.

Conclusions:

The optimal POEGMEA chain length is critical for balancing nanoparticle stability and antibody conjugation efficiency.
A POEGMEA chain length of 13 units provides a good compromise for creating functional bio-nanoconjugates.
These findings enable the development of stable, specific, and bioactive nanoconjugates for flow cytometry and mass cytometry.