Chromatographic separation simulation of metal-chelating peptides from surface plasmon resonance binding parameters

J Sep Sci. 2020 Jun;43(11):2031-2041. doi: 10.1002/jssc.201900882. Epub 2020 Apr 2.

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 immobilized metal ion determined in surface plasmon resonance, both technics are 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 immobilized metal ion affinity chromatography and surface plasmon resonance.

Keywords: chelation; immobilized metal ion affinity chromatography; modeling; peptides; surface plasmon resonance.

MeSH terms

  • Adsorption
  • Chelating Agents / chemistry
  • Chelating Agents / isolation & purification*
  • Chromatography, Affinity
  • Peptides / chemistry
  • Peptides / isolation & purification*
  • Surface Plasmon Resonance*
  • Transition Elements / chemistry
  • Transition Elements / isolation & purification*

Substances

  • Chelating Agents
  • Peptides
  • Transition Elements

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