Polymer Membrane with Glycosylated Surface by a Chemo-Enzymatic Strategy for Protein Affinity Adsorption

Yan Fang,Huiyu Bai,Jingyuan Liu,Ting He,Lingling Fan,Haowei Zhang,Binrui Li,Hao Gao

doi:10.3390/catal10040415

Abstract

Membranes with glycosylated surfaces are naturally biomimetic and not only have excellent surface hydrophilicity and biocompatibility, but have a specific recognition to target biomacromolecules due to the unique chemo-biological properties of their surface carbohydrates; however, they cannot be easily chemically produced on large scales due to the complex preparation process. This manuscript describes the fabrication of a polypropylene membrane with a glycosylated surface by a chemo-enzymatic strategy. First, hydroxyl (OH) groups were introduced onto the surface of microporous polypropylene membrane (MPPM) by UV-induced grafting polymerization of oligo(ethylene glycol) methacrylate (OEGMA). Then, glycosylation of the OH groups with galactose moieties was achieved via an enzymatic transglycosylation by β-galactosidase (Gal) recombinanted from E. coli. The fabricated glycosylated membrane showed surprisingly specific affinity adsorption to lectin ricinus communis agglutinin (RCA120). The chemo-enzymatic route is easy and green, and it would be expected to have wide applications for large-scale preparation of polymer membranes with glycosylated surfaces.

Highlights

Purified biomacromolecules are foundations of the developing biotechnology and pharmaceutical industries [1]
Glycocalyx are carbohydrates present on the cell surface. They are highly hydrated, which protects the cells to avoid attack from other species, and allows the surface to act as a recognition site involving many molecular recognition processes, including virus invasion, cancer
The site- and stereo-selectivity of such enzymatic transglycosylation causes fabrication of the glycosylated surface with specific glycoside linkages (e.g., 95% α(1→6)-linked and 5% α(1→3)-linked polysaccharide branches) and pure anomeric configuration (e.g., α- or β-) according to the results reported in previous studies

Summary

Introduction

Purified biomacromolecules (protein, peptide, nucleic acid, glycan, etc.) are foundations of the developing biotechnology and pharmaceutical industries [1]. The in-service process of the affinity membrane chromatography is essentially based on the specific recognition between the immobilized ligands on the membrane surfaces and the target biomacromolecules. Among all of the studies for the affinity membranes, the glycosylated membrane is a promising one which has been rapidly developed in the last 10 years. The glycosylated membrane is a synthetic membrane with glycocalyx-like surface. Glycocalyx are carbohydrates present on the cell surface. They are highly hydrated, which protects the cells to avoid attack from other species, and allows the surface to act as a recognition site involving many molecular recognition processes, including virus invasion, cancer

Methods

Results

Conclusion