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Issue 30, 2015
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Binding performance of pepsin surface-imprinted polymer particles in protein mixtures

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Abstract

Surface-imprinted polymer particles facilitate the accessibility of synthetic selective binding sites for proteins. Given their volume-to-surface ratio, submicron particles offer a potentially large surface area facilitating fast rebinding kinetics and high binding capacities, as investigated herein by batch rebinding experiments. Polymer particles were prepared with (3-acrylamidopropyl)trimethylammonium chloride as functional monomer, and ethylene glycol dimethacrylate as cross-linker in the presence of pepsin as template molecule via miniemulsion polymerization. The obtained polymer particles had an average particle diameter of 623 nm, and a specific surface area of 50 m2 g−1. The dissociation constant and maximum binding capacity were obtained by fitting the Langmuir equation to the corresponding binding isotherm. The dissociation constant was 7.94 μM, thereby indicating a high affinity; the binding capacity was 0.72 μmol m−2. The binding process was remarkably fast, as equilibrium binding was observed after just 1 min of incubation. The previously determined selectivity of the molecularly imprinted polymer for pepsin was for the first time confirmed during competitive binding studies with pepsin, bovine serum albumin, and β-lactoglobulin. Since pepsin has an exceptionally high content in acidic amino acids enabling strong interactions with positively charged quaternary ammonium groups of the functional monomers, another competitive protein, i.e., α1-acid glycoprotein, was furthermore introduced. This protein has a similarly high content in acidic amino acids, and was used for demonstrating the implications of ionic interactions on the achieved selectivity.

Graphical abstract: Binding performance of pepsin surface-imprinted polymer particles in protein mixtures

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Publication details

The article was received on 10 Apr 2015, accepted on 23 Jun 2015 and first published on 23 Jun 2015


Article type: Paper
DOI: 10.1039/C5TB00657K
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J. Mater. Chem. B, 2015,3, 6248-6254

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    Binding performance of pepsin surface-imprinted polymer particles in protein mixtures

    B. Pluhar, U. Ziener and B. Mizaikoff, J. Mater. Chem. B, 2015, 3, 6248
    DOI: 10.1039/C5TB00657K

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