LAUSR.org creates dashboard-style pages of related content for over 1.5 million academic articles. Sign Up to like articles & get recommendations!

Chromatographic Separation Simulation of Metal-Chelating Peptides from Surface Plasmon Resonance Binding Parameters.

Photo from wikipedia

Some metal-chelating peptides have antioxidant properties, with potential nutrition, health and cosmetics applications. This study aimed to simulate their separation on immobilized metal ion affinity chromatography from their affinity constant… Click to show full abstract

Some metal-chelating peptides have antioxidant properties, with potential nutrition, health and cosmetics applications. This study aimed to simulate their separation on immobilized metal ion affinity chromatography from their affinity constant for immobilised metal ion determined in surface plasmon resonance, both technics being based on peptide-metal ion interactions. In our approach, first, the affinity constant of synthetic peptides was determined by surface plasmon resonance and used as input data to numerically simulate the chromatographic separation with a transport-dispersive model based on Langmuir adsorption isotherm. Then, chromatographic separation was applied on the same peptides to determine their retention time and compare this experimental tR with the simulated tR obtained from simulation from surface plasmon resonance data. For the investigated peptides, the relative values of tR were comparable. Hence, our study demonstrated the pertinence of such numerical simulation correlating immobilised metal ion affinity chromatography and surface plasmon resonance. This article is protected by copyright. All rights reserved.

Keywords: metal; plasmon resonance; chromatographic separation; surface plasmon

Journal Title: Journal of separation science
Year Published: 2020

Link to full text (if available)


Share on Social Media:                               Sign Up to like & get
recommendations!

Related content

More Information              News              Social Media              Video              Recommended



                Click one of the above tabs to view related content.