Preparation method of amphiphilic affinity polymer microspheres with core-shell structure

Abstract

The present invention relates to the preparation of a novel core-shell structure amphiphilic affinity polymer microspheres, comprising the following steps (a) preparing hydrophobic particle poly(divinylbenzene-co-4-vinylphenylboronic acid) by distillation and precipitation method ) microspheres; (b) preparing amphiphilic polymer microspheres with a core-shell structure by means of Pickering emulsion dispersion polymerization. The beneficial effect of the present invention is: (1) the amphoteric nucleophilic polymer of a kind of core-shell structure prepared by the present invention, surface hydrophobic, interior hydrophilic, can be used for under high temperature condition to horseradish peroxidase have better effect. The protection of horseradish peroxidase has better activity and good enzymatic activity. (2) No surfactant is used in the preparation method, which overcomes the problem of difficult removal of traditional surfactants, and will provide an effective means for future research on protein denaturation mechanism.

Description

technical field [0001] The invention belongs to the technology of amphiphilic affinity microspheres with core-shell structure prepared by the Pickering emulsion polymerization method and the research field of protein protection, especially the activity of horseradish peroxidase under high temperature conditions. Background technique [0002] The protein is unstable in vitro and is easily affected by the environment. Under extreme pH conditions, heating, denaturants and organic solvents, the protein structure will be changed, and the hydrophobic groups will be exposed, resulting in the aggregation of protein monomers through hydrophobic interactions. Eventually lead to irreversible denaturation of the protein. Researchers have done a lot of research work on protein protection in vitro, and developed a variety of protein protection reagents, such as surfactants, polymer microspheres, polymeric nanoparticles, polymer micelles, and molecular chaperones. These works have greatly...

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Problems solved by technology

This method also encountered some problems at the same time. On the one hand, according to previous literature reports, protein refolding and irreversible denaturation mainly rely on hydrophobic interactions. If the prepared material is too hydrophobic, it will be difficult to disperse in aqueous solution. If the prepared material is too Hydrophilicity leads to a greatly reduced ability to protect and refold

On the other hand, the hydrophobic groups and hydrophilic groups are randomly distributed in the polymer particles, which brings difficulties to the future research on the denaturation mechanism of proteins.

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