Multilayer affinity adsorption of albumin on polymer brushes modified membranes in a continuous-flow system
| Autor: | Ge-Rui Ren, Ji-Nian Li, Xiang Li, Meng-Xin Hu, Jing-Jing Huang |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Polymers
Surface Properties 02 engineering and technology Plasma protein binding Ligands Polypropylenes 010402 general chemistry Methacrylate 01 natural sciences Biochemistry Chemistry Techniques Analytical Analytical Chemistry Contact angle chemistry.chemical_compound Adsorption Albumins Spectroscopy Fourier Transform Infrared Monolayer chemistry.chemical_classification Chromatography Chemistry Photoelectron Spectroscopy Organic Chemistry Cholic acid Proteins Membranes Artificial General Medicine Polymer 021001 nanoscience & nanotechnology 0104 chemical sciences Membrane Chemical engineering Methacrylates 0210 nano-technology Protein Binding |
| Zdroj: | Journal of Chromatography A. 1538:94-103 |
| ISSN: | 0021-9673 |
| DOI: | 10.1016/j.chroma.2018.01.031 |
| Popis: | Polymer brushes modified surfaces have been widely used for protein immobilization and isolation. Modification of membranes with polymer brushes increases the surface concentration of affinity ligands used for protein binding. Albumin is one of the transporting proteins and shows a high affinity to bile acids. In this work, the modified membranes with cholic acid-containing polymer brushes can be facilely prepared by the immobilization of cholic acid on the poly(2-hydroxyethyl methacrylate) grafted microporous polypropylene membranes (MPPMs) for affinity adsorption of albumin. ATR/FT-IR and X-ray photoelectron spectroscopy were used to characterize the chemical composition of the modified membranes. Water contact angle measurements were used to analyze the hydrophilic/hydrophobic properties of the membrane surface. The modified MPPMs show a high affinity to albumin and have little non-specific adsorption of hemoglobin. The dynamic binding capacity of albumin in the continous-flow system increases with the cycle number and feed rate as the binding degree of cholic acid is moderate. The highest binding capacity of affinity membranes is about 52.49 g/m2 membrane, which is about 24 times more than the monolayer binding capacity. These results reveal proteins could be captured in multilayers by the polymer brushes containing affinity ligands similar to the polymer brushes containing ion-exchange groups, which open up the potential of the polymer brushes containing affinity ligands in protein or another components separation. And the cholic acid containing polymer brushes modified membranes has the promising potential for albumin separation and purification rapidly from serum or fermented solution in medical diagnosis and bioseparation. |
| Databáze: | OpenAIRE |
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