One-Step Surface Immobilization of Protein A on Hydrogel Nanofibers by Core-Shell Electrospinning for Capturing Antibodies

Nanofibers (NFs) are potential candidates as filter materials for affinity separation owing to their high liquid permeability based on their high porosity. Multiple and complex processes were conventionally performed to immobilize proteins for modifying NF surfaces. A simple method must be developed...

Full description

Saved in:

Bibliographic Details
Published in:	International journal of molecular sciences Vol. 22; no. 18; p. 9857
Main Authors:	Naganuma, Chihiro, Moriyama, Kosuke, Suye, Shin-Ichiro, Fujita, Satoshi
Format:	Journal Article
Language:	English
Published:	Switzerland MDPI AG 12-09-2021 MDPI
Subjects:	Acetic acid Adsorption Affinity Antibodies Aqueous environments Biological activity Cellulose - analogs & derivatives Cellulose acetate Chromatography Electrospinning Flow velocity Hydrogels Immobilization Laboratories Ligands membrane chromatography Membranes Microprocessors Morphology nanofiber Nanofibers Nanofibers - chemistry Nanotechnology - methods Permeability Polymers Polyvinyl alcohol Porosity Protein A Proteins Staphylococcal Protein A surface modification United States > US Japan protein A electrospinning surface modification membrane chromatography nanofiber
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	Nanofibers (NFs) are potential candidates as filter materials for affinity separation owing to their high liquid permeability based on their high porosity. Multiple and complex processes were conventionally performed to immobilize proteins for modifying NF surfaces. A simple method must be developed to immobilize proteins without impairing their biological activity. Herein, we succeeded in fabricating NFs with a core of cellulose acetate and a shell of hydrophilic polyvinyl alcohol immobilized with staphylococcal recombinant protein A by a one-step process based on core-shell electrospinning. A total of 12.9 mg/cm of antibody was captured in the fiber shell through high affinity with protein A immobilized in an aqueous environment of the hydrogel. The maximum adsorption site and dissociation constant evaluated by the Langmuir model were 87.8 µg and 1.37 µmol/L, respectively. The fiber sheet withstood triplicate use. Thus, our NF exhibited high potential as a material for membrane chromatography.
ISSN:	1422-0067 1661-6596 1422-0067
DOI:	10.3390/ijms22189857