An effective way to imprint protein with the preservation of template structure by using a macromolecule as the functional monomer

Abstract

In this study, an assumption that a micromolecular monomer could easily permeate into the inside of a protein and alter its conformation, while an inflexible macromolecular monomer may interact with the surface of the protein and thus maintain the integrity of the template protein's structure was proposed for the first time and confirmed by using circular dichroism and synchronous fluorescence spectroscopy. The protein imprinted hydrogels composed of macromolecular monomers or their equivalent micromolecular monomers were characterized and carried out in the competitive adsorption and adsorption isotherm experiments. The adsorption isotherm behaviours described by the Langmuir model revealed that a higher binding affinity was observed between the template protein and imprinted hydrogels made by a macromolecular monomer. The competitive adsorption results also demonstrated the imprinted hydrogels prepared by the macromolecular monomer exhibited much better specific recognition ability to the template protein. Therefore, the strategy of using a macromolecule to imprint could effectively overcome the mutability of protein during the preparation of imprinted polymers, and consequently would promote the development of imprinting technology.Scheme 1 The influence of macromolecular chain and micromolecular monomer on the conformation of template protein.

Molecularly Imprinted Silk Fibroin Nanoparticles

“… 5 , 7 , 11 With the purpose of forming stable, yet molecularly imprinted, SF-NPs, methacrylated fibroin (SF-MA) 28 was chosen as the macromolecular monomer. 29 SF-MA, also known as Sil-MA, 28 possesses reactive pendant double bonds that permit cross-linking of the formed SF-NPs, hence, their stabilization. The cross-linking of the SF-NPs occurred via UV-induced photo-cross-linking by means of lithium phenyl- 2,4,6-trimethylbenzoyl phosphinate (LAP).…”

Molecularly Imprinted Materials for Selective Biological Recognition

“…Moreover, temperature‐sensitive hydrogel was chosen as imprinted substrate here for its milder preparation condition and easier template‐elution process ( Figure A). Another work showed that using macromolecular monomer instead to stabilize protein conformation . Based on different flexibility and mobility between macromolecule and its corresponding micromolecule, Qian designed a linear macromolecular chain composed of imidazole and polymerizable ionic acid unit.…”

“…Copyright 2014, Elsevier; B) different effects of monomers and macromolecular chain on the secondary structure of proteins. Reproduced with permission . Copyright 2015, Royal Society of Chemistry; C) recognition process of epitope mimetic peptide imprinting nanoparticles for p32.…”

“…Another work showed that using macromolecular monomer instead to sta bilize protein conformation. [148] Based on different flexibility and mobility between macromolecule and its corresponding micromolecule, Qian designed a linear macromolecular chain composed of imidazole and polymerizable ionic acid unit. Better recognition ability of imprinted hydrogel including macro molecular chain than that of micromolecular with same composition and usage was achieved.…”

“…Reproduced with permission. [148] Copyright 2015, Royal Society of Chemistry; C) recognition process of epitope mimetic peptide imprinting nanoparticles for p32. Reproduced with permission.…”