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Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

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Updated: Aug 14, 2025

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

Optimized Coiled-Coil Interactions for Multiplexed Peptide-PAINT.

Alexandra S Eklund^1,2, Ralf Jungmann^1,2

¹Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Planegg, Germany.

Small (Weinheim an Der Bergstrasse, Germany)

|January 16, 2023

Summary

This summary is machine-generated.

Researchers enhanced Peptide-PAINT super-resolution microscopy by optimizing peptide binding kinetics and introducing a new peptide pair for multiplexed imaging. This advancement enables 2-color imaging of proteins like ErbB2/Her2 at the single-molecule level.

Keywords:

DNA origami DNA points accumulation for imaging in nanoscale topography cell receptor imaging coiled-coil interactions peptide points accumulation for imaging in nanoscale topography single molecules super-resolution imaging

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Area of Science:

Biophysics
Molecular Biology
Microscopy

Background:

Super-resolution microscopy, including DNA-PAINT, allows nanoscale imaging in life sciences.
Peptide-PAINT offers improved labeling for target proteins by using peptide interactions instead of DNA oligonucleotides.
Current Peptide-PAINT methods are limited to a single imaging channel, hindering multiplexing.

Purpose of the Study:

To optimize the existing Peptide-PAINT E/K coil for enhanced binding kinetics and localization precision.
To develop and validate an orthogonal peptide pair (P3/P4) for multiplexed Peptide-PAINT.
To demonstrate the utility of 2-plex Peptide-PAINT for imaging biological targets at the single-receptor level.

Main Methods:

Modification of the Peptide-PAINT E/K coil length to improve binding kinetics.
Introduction and characterization of an orthogonal P3/P4 coiled-coil peptide pair.
Performance evaluation using single-molecule and DNA origami assays, and imaging of ErbB2/Her2 receptors.

Main Results:

Optimized E/K coil demonstrated improved localization precision.
The novel P3/P4 peptide pair showed high orthogonality and enabled 2-plex Peptide-PAINT.
Successful 2D and 3D imaging of human epidermal growth factor receptors 2 (ErbB2/Her2) at the single-receptor level was achieved.

Conclusions:

Optimized peptide sequences and novel orthogonal pairs significantly advance Peptide-PAINT capabilities.
2-plex Peptide-PAINT opens new avenues for multiplexed super-resolution imaging in biological systems.
This technique allows high-resolution visualization of protein targets like ErbB2/Her2 in their native cellular context.