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Monitoring Conformational Dynamics of Single Unmodified Proteins using Plasmonic Nanotweezers

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Exploring transferrin-receptor interactions at the single-molecule level.

Alexandre Yersin¹, Toshiya Osada, Atsushi Ikai

¹Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Kanagawa, Japan. ayersin@bio.titech.ac.jp

Biophysical Journal

|September 18, 2007

Summary

This summary is machine-generated.

The transferrin-transferrin receptor interaction differs significantly based on iron binding. Holo-transferrin binding to its receptor requires more force and involves two energy barriers for dissociation compared to apo-transferrin.

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Area of Science:

Biochemistry
Cell Biology
Biophysics

Background:

The transferrin (Tf) and transferrin receptor (TfR) system is crucial for cellular iron uptake in most organisms.
TfR binds iron-loaded Tf (holo-Tf), internalizes it into endosomes for iron release, and recycles iron-free Tf (apo-Tf) back to the cell surface.

Purpose of the Study:

To investigate the single-molecule biophysics of the Tf-TfR interaction under conditions mimicking the Tf cycle.
To compare the binding and dissociation dynamics of holo-Tf-TfR and apo-Tf-TfR interactions.

Main Methods:

Utilized atomic force microscopy (AFM) with functionalized tips to probe TfR.
Measured dynamic forces of interaction between holo-Tf and apo-Tf with TfR.
Examined TfR both purified on mica substrates and in situ on living cells.

Main Results:

Single-molecule force measurements revealed distinct interaction profiles for holo-Tf-TfR versus apo-Tf-TfR.
The holo-Tf-TfR interaction exhibited significantly higher unbinding forces compared to the apo-Tf-TfR interaction.
Dissociation of the holo-Tf-TfR complex involved overcoming two energy barriers, while apo-Tf-TfR dissociation involved only one.

Conclusions:

The biophysical properties of the Tf-TfR interaction are modulated by the iron-binding state of transferrin.
The findings support a model where holo-Tf and apo-Tf engage TfR through different contact points, influencing interaction strength and dissociation pathways.