Abstract
In this work the adsorption of tri-peptides on a mixed-mode resin was studied using isocratic pulse response experiments. Various salt concentration, temperature and pH combinations were used to measure retention times of several tri-peptides. The experiments were evaluated according to an extension of the stoichiometric displacement model and the steric mass action model of protein-ligand binding. The application of this model in the understanding of mixed mode adsorption process is discussed. A unique set of meaningful thermodynamic parameters was obtained for each resin-peptide-temperature and resin-peptide-pH combination. Finally it was shown that these thermodynamic parameters can be used in defining quantitative relationships within the framework of extra thermodynamic relationships.
| Original language | English |
|---|---|
| Pages (from-to) | 41-49 |
| Number of pages | 9 |
| Journal | Journal of Chromatography A |
| Volume | 1341 |
| DOIs | |
| Publication status | Published - 9 May 2014 |
| Externally published | Yes |
Keywords
- Gibbs free energy
- Mixed-mode chromatography
- Peptide adsorption
- Thermodynamic modelling
- Tri-peptides
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