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Updated: Mar 11, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Profiling Phosphopeptide-Binding Domain Recognition Specificity Using Peptide Microarrays.

Michele Tinti¹, Simona Panni², Gianni Cesareni^3,4

¹Division of Biochemical Chemistry and Drug Discovery, College of Life Science, Dundee University, Dow Street, Dundee, DD1 4HN, UK. m.tinti@dundee.ac.uk.

Methods in Molecular Biology (Clifton, N.J.)

|November 23, 2016

Summary

This summary is machine-generated.

Understanding protein phosphorylation is key to cellular signaling. This study presents a peptide array method to precisely map the binding specificities of phosphopeptide recognition domains, crucial for deciphering protein interaction networks.

Keywords:

14-3-3 Binding domains Interaction networks Phosphopeptide SH2 Spot synthesis

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Last Updated: Mar 11, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

Analysis of Histone Antibody Specificity with Peptide Microarrays

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Specificity Analysis of Protein Lysine Methyltransferases Using SPOT Peptide Arrays

Published on: November 29, 2014

Area of Science:

Molecular Biology
Cellular Biology
Biochemistry

Background:

Cellular processes rely on complex protein interactions.
Post-translational modifications, like phosphorylation, regulate these interactions.
Phosphorylation is vital in signal transduction, affecting enzyme activity and complex formation.

Purpose of the Study:

To define the binding specificity of phosphopeptide recognition domains.
To understand the interaction web mediated by phosphopeptides.
To present a reliable method for studying phosphoprotein interactions.

Main Methods:

Development of a protocol to assemble large-scale phospho-peptide arrays.
Screening of these arrays with modular protein domains (e.g., SH2, PTB, 14-3-3).
Utilizing peptide arrays as a powerful approach for identifying binding preferences.

Main Results:

Demonstration of a method to create arrays of hundreds to thousands of phospho-peptides.
Enabling the screening of these arrays with various modular domains of interest.
Precise identification of binding preferences for phosphopeptide recognition domains.

Conclusions:

Peptide arrays are effective for studying interactions involving phosphorylated proteins.
Accurate recognition of phosphorylation sites is essential for understanding cellular signaling.
This protocol facilitates the inference of the phosphopeptide-mediated interaction network.