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Modification and Functionalization of the Guanidine Group by Tailor-made Precursors

Modification and Functionalization of the Guanidine Group by Tailor-made Precursors

Published on: April 27, 2017

Guanidinium Pairing Facilitates Membrane Translocation.

Christoph Allolio^1,2, Katarina Baxova¹, Mario Vazdar³

¹Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences , Flemingovo nám. 2, CZ-166 10 Prague 6, Czech Republic.

The Journal of Physical Chemistry. B

|December 18, 2015

Summary

Like-charge guanidinium ion pairs are stable in water and lipid bilayers, facilitating ion presence within membranes. This phenomenon can lead to pore formation and impact cell-penetrating peptides and ion conduction.

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Area of Science:

Computational chemistry
Biophysics
Physical chemistry

Background:

Like-charge ion pairing is generally considered unfavorable in aqueous solutions.
Understanding ion behavior within lipid bilayers is crucial for membrane function and drug delivery.

Purpose of the Study:

To investigate the thermodynamic stability of guanidinium ion pairing in aqueous solution and within a lipid bilayer.
To elucidate the role of like-charge ion pairing in ion transfer across membranes and its contribution to membrane structure.

Main Methods:

Ab initio free energy calculations were employed to study guanidinium ion interactions.
Free energy decomposition was used to quantify ion transfer contributions.
Comparisons were made with ammonium ions to highlight specific guanidinium properties.

Main Results:

The study confirms the thermodynamic stability of like-charge guanidinium ion pairs in aqueous solution.
Like-charge guanidinium ion pairing also occurs within lipid bilayer defects, contributing to ion transfer nonadditivity.
This pairing facilitates ion presence inside the bilayer and can lead to pore formation.

Conclusions:

Like-charge ion pairing of guanidinium ions is a significant factor influencing their behavior in both bulk solution and lipid membranes.
The findings have implications for understanding ion transport, membrane integrity, and the mechanisms of cell-penetrating peptides.