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Liquid-Liquid Phase Separation As the Second Step of Complex Coacervation.

Aditya N Singh¹, Arun Yethiraj¹

¹Theoretical Chemistry Institute and Department of Chemistry, 1101 University Avenue, University of Wisconsin-Madison, Madison, Wisconsin 53703, United States.

The Journal of Physical Chemistry. B

|March 18, 2021

Summary

Arginine- and tyrosine-rich peptides drive liquid-liquid phase separation (LLPS) through energetically favorable complexation. This process, driven by π-cation bonds, resembles neutral polyion pair separation, not complex coacervation.

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Area of Science:

Biochemistry
Biophysics
Computational Biology

Background:

Liquid-liquid phase separation (LLPS) is crucial for cellular organization.
Understanding the molecular mechanisms of LLPS, particularly in relation to protein-protein interactions, is essential.

Purpose of the Study:

To investigate the interactions between tyrosine- and arginine-rich peptides in a condensed phase.
To elucidate the mechanism of complexation and its relation to LLPS and complex coacervation.

Main Methods:

Multiple umbrella sampling calculations were performed on oligomers containing tyrosine (pY) and arginine (pR).
Metadynamics simulations were used to study monomer interactions and correlate complexation energy with π-cation bonds.
Free energy calculations were conducted on polyglutamate-pR dimer pairs.

Main Results:

Complexation between pR and pY peptides is energetically favorable.
The energy of complexation correlates with the number of π-cation bonds formed.
The binding process between polyglutamate-pR dimers shows similarities to LLPS.

Conclusions:

Proteins rich in arginine and tyrosine do not follow a complexation-then-coacervation mechanism for LLPS.
The observed LLPS mechanism is analogous to the phase separation of neutral polyion pairs.