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Reference type: Journal
Authors: Pluhar B, Ziener U, Mizaikoff B
Article Title: Binding performance of pepsin surface-imprinted polymer particles in protein mixtures.
Publication date: 2015
Journal: Journal of Materials Chemistry B
Volume: 3
Issue: (30)
Page numbers: 6248-6254.
DOI: 10.1039/C5TB00657K
Alternative URL: https://www.researchgate.net/publication/279069865_Binding_performance_of_pepsin_surface-imprinted_polymer_particles_in_protein_mixtures

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
Template and target information: protein, pepsin

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