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Updated: Jan 18, 2026

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

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Published on: August 21, 2019

Optimization of CEST MRI Reporter Protein Design Using Cation-Pi Networks.

David E Korenchan¹, Ethan J French¹, Emerenziana Runco²

¹Athinoula A. Martinos Center for Biomedical Imaging, Massachusetts General Hospital, Charlestown, MA, 02129, USA.

Chemistry (Weinheim an Der Bergstrasse, Germany)

|September 10, 2025

Summary

This summary is machine-generated.

Researchers identified novel protein biomarkers for enhanced MRI tracking of gene and viral therapies. These biomarkers offer high specificity and sensitivity, improving in vivo monitoring capabilities.

Keywords:

cation‐pi interaction chemical exchange saturation transfer magnetic resonance imaging nuclear magnetic resonance spectroscopy reporter proteins

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Published on: April 9, 2018

Area of Science:

Biomedical Imaging
Molecular Biology
Therapeutic Development

Background:

Nucleic acid-based therapies require noninvasive methods for tracking delivery, persistence, and spread.
Chemical Exchange Saturation Transfer (CEST) reporter proteins offer high sensitivity for MRI detection.
Existing CEST reporter proteins lack specificity due to overlapping signals with endogenous proteins.

Purpose of the Study:

To investigate proteins and peptides with tyrosine, tryptophan, and lysine residues for enhanced MRI reporter gene applications.
To identify biomarkers that provide distinct CEST contrast away from endogenous signals for improved specificity.
To enable noninvasive in vivo monitoring of viral and gene therapies using MRI.

Main Methods:

Screening of proteins and peptides containing tyrosine, tryptophan, and lysine residues.
Analysis of chemical exchange saturation transfer (CEST) properties, including downfield shifts (4-10 ppm) and exchange rates (400-2500 s⁻¹).
Investigation of molecular interactions, such as hydrogen bonding and cation-π networks, influencing CEST contrast.

Main Results:

Identified molecules exhibiting significant downfield CEST contrast, distinct from water resonance.
Demonstrated detectable exchangeable proton signals from tyrosine, tryptophan, and lysine under physiological conditions.
Attributed observed CEST properties to unique hydrogen bonding and cation-π network interactions.

Conclusions:

Discovered novel protein and peptide candidates for highly specific and sensitive MRI reporter genes.
These findings pave the way for developing stable reporter proteins for advanced in vivo monitoring.
The developed biomarkers will significantly advance the tracking of nucleic acid-based therapies like gene and virotherapy.