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Updated: Oct 24, 2025

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

CRISPR-based peptide library display and programmable microarray self-assembly for rapid quantitative protein binding

Karl W Barber¹, Ellen Shrock¹, Stephen J Elledge¹

¹Division of Genetics, Brigham and Women's Hospital, Howard Hughes Medical Institute, Boston, MA 02115, USA; Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.

|August 14, 2021

Summary

Researchers developed a CRISPR-based peptide display technology for high-throughput protein interaction studies. This system uses catalytically inactive Cas9 (dCas9) to assemble peptide libraries on DNA microarrays for rapid binding assays and diagnostics.

Keywords:

CRISPR Cas9 FLAG SARS-CoV-2 antibody binding influenza A protein display protein microarray protein-protein interactions self-assembly

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Last Updated: Oct 24, 2025

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Kinase Inhibitor Screening In Self-assembled Human Protein Microarrays

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Area of Science:

Molecular Biology
Biotechnology
Genomics

Background:

CRISPR-inspired systems are widely used for genome editing and nucleic acid detection.
Existing methods for studying protein interactions can be limited in throughput and customization.
There is a need for advanced tools to facilitate high-throughput in vitro protein interaction studies.

Purpose of the Study:

To introduce a novel CRISPR-based peptide display technology for customized, high-throughput in vitro protein interaction studies.
To demonstrate the utility of this platform for antibody-epitope binding characterization and viral epitope mapping.
To explore its potential as a multiplexed diagnostics tool.

Main Methods:

Developed peptide libraries fused to catalytically inactive Cas9 (dCas9) and barcoded with single guide RNA (sgRNA).
Utilized self-assembly of these libraries to programmable positions on a DNA microarray surface.
Employed dCas9-displayed saturation mutagenesis libraries for antibody-epitope binding assays.

Main Results:

Successfully demonstrated rapid, multiplexed binding assays using the CRISPR-based peptide display platform.
Characterized antibody-epitope binding for a commercial antibody and human serum antibodies using saturation mutagenesis libraries.
Showcased the platform's capability for viral epitope mapping and its promise as a multiplexed diagnostics tool.

Conclusions:

The CRISPR-based peptide display technology enables customized, high-throughput in vitro protein interaction studies.
The platform facilitates rapid interrogation of protein libraries and has potential applications in diagnostics.
The principles of dCas9-mediated library self-assembly using DNA scaffolding can be adapted for diverse biological applications.