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Related Experiment Video

Updated: Jun 26, 2026

Glycopeptide Capture for Cell Surface Proteomics

Glycopeptide Capture for Cell Surface Proteomics

Published on: May 9, 2014

Peptide pore accessibility in reversed-phase chromatography.

David Gétaz¹, Guido Ströhlein, Massimo Morbidelli

¹Department of Chemistry and Applied Bioscience, Institute for Chemical and Bioengineering, ETH Zurich, CH-8093 Zurich, Switzerland.

Journal of Chromatography. A

|December 30, 2008

Summary

Peptide porosity increases with local negative charge concentration, impacting chromatographic peak shapes. This phenomenon, observed in reversed-phase chromatography, can be modeled using non-constant porosity assumptions.

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Glycopeptide Capture for Cell Surface Proteomics

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Published on: May 9, 2014

Sample Preparation for Endopeptidomic Analysis in Human Cerebrospinal Fluid

Sample Preparation for Endopeptidomic Analysis in Human Cerebrospinal Fluid

Published on: December 4, 2017

Area of Science:

Analytical Chemistry
Chromatography Science

Background:

Reversed-phase chromatography is a key separation technique.
Understanding the factors affecting pore accessibility is crucial for optimizing separations.

Purpose of the Study:

To investigate the impact of salt and peptide concentration on peptide porosity.
To explore the relationship between stationary phase properties and peptide accessibility.

Main Methods:

Studied six reversed-phase stationary phases.
Measured peptide porosity and acetonitrile adsorption isotherms.
Utilized an ideal chromatography model with non-constant porosity.

Main Results:

Peptide porosity increases with local negative charge concentration in a saturable manner.
Observed anti-Langmuirian peaks due to increased ionic strength enhancing porosity.
Correlated acetonitrile adsorption with reduced peptide pore accessibility.

Conclusions:

Peptide concentration and ionic strength significantly influence peptide porosity in reversed-phase chromatography.
The observed behavior can be accurately modeled by considering non-constant porosity.
Stationary phase properties, like acetonitrile adsorption, affect peptide accessibility.