Macroporous Thermosensitive Imprinted Hydrogel for Recognition of Protein by Metal Coordinate Interaction

Abstract

A thermosensitive macroporous hydrogel showing selectivity for the lysozyme was developed by an imprinting procedure that is based on metal coordinate interaction. A metal chelate monomer [N-(4-vinyl)-benzyl iminodiacetic acid] forming coordination complex with the template protein in the presence of Cu ions co-polymerized with N-isopropylacrylamide and acrylamide, using N,N-methylenebisacrylamide as the cross-linker to prepare the thermosensitive protein-imprinted hydrogel. The synergetic combination of the smart property of the macroporous thermosensitive hydrogel with the merits of the coordinate interaction improved the selectivity and adsorption capacity, with respect to template lysozyme. The macropores were created by the frozen polymerization, and the influences of frozen polymerization and the chelate monomer content on the hydrogel affinity were investigated. The imprinted hydrogel can respond not only to external stimuli, but also to the template protein with a certain degree of shrinking. In recognition of the protein, the interaction of the imprinted thermosensitive hydrogel to the protein can be switched between the coordinate effect and the electrostatic effect by adding or not adding Cu ions. Finally, this imprinted hydrogel was used to purify the template lysozyme from the mixture of proteins and the real sample, which demonstrated its high selectivity.

A Thermosensitive Monolithic Column as an Artificial Antibody for the On‐line Selective Separation of the Protein

“…[26][27][28] This kind of stimuli-sensitive recognition is very similar to the recognition of proteins in natural systems. [29][30][31] So far, to the best of our knowledge, the preparation of a thermosensitive polymer to imprint a protein has been limited to static formats, such as our previous study on the bulk polymerization of a macroporous thermosensitive imprinted hydrogel for the recognition of proteins, [32] and has not been applied to monolithic columns for proteins. [33][34][35][36] This study focuses on the combined merits of the monolithic column and the thermosensitive protein MIP to selectively separate a template protein in an on-line method.…”

Current status and challenges of ion imprinting

“…At 28 C, the imprinting cavity was in a swollen state and the monomer chelated with Cu(II), which was easily accessible for the protein, leading to the maximum adsorption capacity. 81 When the temperature increased to 43 C, the cavity was in a collapsed state and the Cu(II) was blocked, resulting in a lower adsorption of the protein. 81 However, dual/multi-stimuli responsive imprinted polymers are relatively less explored for ions than molecules.…”

Deposition of fluorescent NIPAM-based nanoparticles on solid surfaces: Quantitative analysis and the factors affecting it

“…Qin et al (3) prepared a p(NIPAM) nanoparticle with a metal chelate comonomer N- (4-vinyl)-benzyl iminodiacetic acid. In the presence of Cu 2+ ions, this comonomer forms a co-ordination complex with the template protein.…”

“…The authors suggest the new method will be suitable for the separation of charged biomolecules such as proteins, DNA and peptides, and they refer to this technique as 'temperature responsive chromatography'. M a n u s c r i p t 3 The work reported herein aims to determine the quantity of nanoparticles deposited on different surfaces under specified conditions and to discuss the factors affecting it (substrate surface charge, surface roughness, hydrophilicity/hydrophobicity and the temperature at which the deposition/desorption processes take place. This is important to move the applications of stimuli responsive surfaces from the research phase to the practical application one with special consideration to the commercial factors associated with this process.…”