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Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay PCA in Living Cells

Published on: March 3, 2015

Parallel force assay for protein-protein interactions.

Daniela Aschenbrenner¹, Diana A Pippig², Kamila Klamecka³

¹Lehrstuhl für Angewandte Physik and Center for Nanoscience (CeNS), Ludwig-Maximilians-; Munich Center for Integrated Protein Science (CIPSM), Butenandtstr. 5-13, 81377 Munich, Germany.

|December 30, 2014

Summary

This summary is machine-generated.

This study introduces a DNA-based Molecular Force Assay to quantify protein-protein interactions, specifically between GFP variants and nanobodies. The assay effectively measures binding forces, revealing differences in nanobody binding to various GFP constructs.

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Area of Science:

Biochemistry
Molecular Biology
Biophysics

Background:

High-resolution parallel assays are crucial for quantitative proteome research.
Characterizing protein complexes by binding forces offers wide dynamic range and distinguishes non-specific interactions.

Purpose of the Study:

To present a DNA-based Molecular Force Assay for quantifying protein-protein interactions.
To investigate the binding dynamics between Green Fluorescent Protein (GFP) variants and GFP-binding nanobodies.
To explore strategies for adjusting assay sensitivity by modifying DNA reference duplexes.

Main Methods:

Development of a DNA-based Molecular Force Assay.
Quantification of binding forces between different GFP variants and GFP-binding nanobodies.
Adjustment of assay sensitivity by altering DNA binding strength.

Main Results:

The assay successfully quantified interactions between GFP variants and nanobodies.
Nanobody Enhancer binding to wild type and enhanced GFP showed equal strength within experimental error.
Stronger binding of Nanobody Enhancer to superfolder GFP was observed and attributed to specific amino acid alterations.

Conclusions:

The DNA-based Molecular Force Assay provides a sensitive method for quantifying protein-protein interactions.
Observed binding differences correlate with structural variations in GFP variants.
The assay demonstrates potential for large-scale parallelization in quantitative proteome research.