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Electrophoretic mobilities and migrating analytes: Part 1: Relationships.

Reginald F Cross¹, Margaret G Wong

¹School of Engineering and Science, Environment & Biotechnology Centre, Swinburne University of Technology, Hawthorn, Victoria, Australia. rcross@swin.edu.au

Journal of Capillary Electrophoresis and Microchip Technology

|January 28, 2003

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Molecular modeling determined peptide radii, revealing electrophoretic mobility is proportional to 1/r², correcting textbook inaccuracies. This finding impacts peptide analysis and understanding of molecular interactions.

Area of Science:

Biophysical Chemistry
Computational Chemistry
Molecular Modeling

Background:

Electrophoretic mobility (mu(ep)) is a crucial parameter in analyzing peptides and proteins.
Existing models often simplify the relationship between molecular size and mobility.
Textbook descriptions of electrophoretic mobility dependence on molecular radius (r) may be inaccurate.

Purpose of the Study:

To accurately determine the molecular radii of peptides using computational methods.
To investigate the precise relationship between peptide molecular radius and electrophoretic mobility.
To correct and refine the understanding of electrophoretic mobility in relation to molecular size.

Main Methods:

Utilized molecular modeling techniques to calculate the molecular radii (r) for a series of peptides.

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Analyzed the correlation between the determined molecular radii and experimentally or theoretically derived electrophoretic mobility values.

Compared the findings with established theoretical equations, including the Offord equation.

Main Results:

Demonstrated that electrophoretic mobility (mu(ep)) is directly proportional to the inverse square of the molecular radius (mu(ep) proportional to 1/r²).
Showed that the commonly cited inverse linear relationship (mu(ep) proportional to 1/r) is incorrect for peptides.
Evaluated the applicability and limitations of the mass-based Offord equation in this context.

Conclusions:

The relationship between peptide molecular radius and electrophoretic mobility is quadratic, not linear.
Accurate molecular radii are essential for precise electrophoretic mobility predictions.
This study refines theoretical models for peptide electrophoresis and molecular characterization.