The role of ligands on protein retention in adsorption chromatography: A surface energetics approach

Protein adsorption onto hydrophobic chromatographic supports has been investigated using a colloid theory surface energetics approach. The surface properties of commercially available chromatographic beads, Toyopearl Phenyl 650‐C, and Toyopearl Butyl 650‐C, have been experimentally determined by con...

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Bibliographic Details
Published in:Journal of separation science 2014-03, Vol.37 (6), p.618-624
Main Authors: Aasim, Muhammad, Kakarla, Prasad Babu, D'Souza, Roy N., Bibi, Noor Shad, Klein, Tanja Yvonne, Treccani, Laura, Rezwan, Kurosch, Fernández-Lahore, Marcelo
Format: Article
Language:English
Subjects:
Adsorption
Adsorption chromatography
Analytical, structural and metabolic biochemistry
Animals
Beads
Biological and medical sciences
Cattle
Chickens
Chromatography
Chromatography, Liquid
Fundamental and applied biological sciences. Psychology
General aspects, investigation methods
Hydrophobic interactions
Ligands
Mathematical models
Muramidase - chemistry
Muramidase - metabolism
Phenyls
Protein adsorption
Proteins
Serum Albumin, Bovine - chemistry
Serum Albumin, Bovine - metabolism
Surface chemistry
Surface energetics
Surface Properties
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Summary:Protein adsorption onto hydrophobic chromatographic supports has been investigated using a colloid theory surface energetics approach. The surface properties of commercially available chromatographic beads, Toyopearl Phenyl 650‐C, and Toyopearl Butyl 650‐C, have been experimentally determined by contact angle and zeta potential measurements. The adsorption characteristics of these beads, which bear the same backbone matrix but harbor different ligands, have been studied toward selected model proteins, in the hydrated as well as dehydrated state. There were two prominent groups of proteins observed with respect to the chromatographic supports presented in this work: loosely retained proteins, which were expected to have lower average interaction energies, and the strongly retained proteins, which were expected to have higher average interaction energies. Results were also compared and contrasted with calculations derived from adsorbent surface energies determined by inverse liquid chromatography. These results showed a good qualitative agreement, and the interaction energy minima obtained from these extended Derjaguin, Landau, Verwey and Overbeek calculations were shown to correlate well with the experimentally determined adsorption behavior of each protein.
ISSN:1615-9306
1615-9314
DOI:10.1002/jssc.201301338