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Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

Isotope-coded ATP probe for quantitative affinity profiling of ATP-binding proteins.

Yongsheng Xiao¹, Lei Guo, Yinsheng Wang

¹Department of Chemistry, University of California, Riverside, California 92521-0403, United States.

Analytical Chemistry

|July 12, 2013

Summary

A new isotope-coded ATP-affinity probe (ICAP) enables quantitative profiling of ATP-binding proteins. This method identifies known and novel ATP-binding sites and proteins across the proteome.

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A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation

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Published on: September 24, 2012

Area of Science:

Proteomics
Biochemistry
Molecular Biology

Background:

ATP-binding proteins are crucial for cellular functions.
Accurate identification of ATP-binding proteins and sites is essential for understanding cellular processes.

Purpose of the Study:

To introduce a novel isotope-coded ATP-affinity probe (ICAP) for quantitative proteomic analysis of ATP-binding proteins.
To develop an affinity profiling strategy for comprehensive characterization of ATP-protein interactions.
To identify novel ATP-binding sites and proteins.

Main Methods:

Development and application of an isotope-coded ATP-affinity probe (ICAP).
Quantitative affinity profiling strategy for proteome-wide analysis.
Minimization of false positives by comparing labeling behaviors at different reagent concentrations.

Main Results:

Validated 258 known ATP-binding proteins in HeLa-S3 and Jurkat-T cells.
Identified a new ATP-binding site (K356) in Heat Shock Protein 90 (HSP90).
Predicted 293 proteins as potential ATP binders and confirmed ATP-binding in human proliferating cell nuclear antigen (PCNA).

Conclusions:

The ICAP approach provides a quantitative and broadly applicable method for assessing ATP-binding proteins.
This strategy effectively identifies known and novel ATP-binding proteins and sites.
The findings expand the understanding of ATP-protein interactions in cellular systems.