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Colloidal model of lysozyme aqueous solutions: a computer simulation and theoretical study.

Giuseppe Pellicane¹

¹School of Chemistry and Physics, University of Kwazulu-Natal, Private Bag X01, Scottsville 3209, Pietermaritzburg, South Africa. pellicane@ukzn.ac.za

The Journal of Physical Chemistry. B

|January 27, 2012

Summary

Derjaguin-Landau-Verwey-Overbeek (DLVO) theory models lysozyme interactions in water. While qualitatively accurate at low ionic strength, DLVO theory becomes quantitative at higher strengths, predicting protein aggregation at elevated pH.

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Area of Science:

Physical chemistry
Biophysics
Computational modeling

Background:

Understanding protein-protein interactions is crucial in biophysics.
The Derjaguin-Landau-Verwey-Overbeek (DLVO) theory is a fundamental model for describing interparticle forces.
Lysozyme is a well-studied model protein for interaction studies.

Purpose of the Study:

To model lysozyme interactions in aqueous solutions using DLVO theory.
To investigate the influence of pH and ionic strength on lysozyme interactions.
To compare theoretical predictions with experimental small-angle neutron scattering data.

Main Methods:

Utilizing Monte Carlo computer simulations to calculate structural functions.
Employing integral equation theories for theoretical analysis.
Comparing calculated scattered intensities with experimental small-angle neutron scattering data.

Main Results:

DLVO theory qualitatively captures the shift towards short-range, attractive interactions at low ionic strength.
DLVO theory becomes quantitatively accurate for lysozyme interactions at sufficiently high ionic strength.
At higher pH values, DLVO theory predicts protein aggregate formation due to competing forces.

Conclusions:

DLVO theory provides a valuable framework for understanding lysozyme interactions, particularly at higher ionic strengths.
The interplay between short-range attraction and long-range repulsion governs protein aggregation.
Computational and theoretical methods, validated by experiments, are key to elucidating complex biomolecular interactions.