Protein recognition onto silica particles using chitosan as intermedium substrate

A novel molecular imprinting method was used to prepare twice‐coated silica particles with specific recognition sites for hemoglobin. Chitosan was used as an intermedium to be coated on silica particles via phase inversion process, and the abundance of exposed amine groups (NH2) were active sites fo...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biomedical materials research. Part A 2009-08, Vol.90A (2), p.326-332
Main Authors: Xia, Yong-Qing, Guo, Tian-Ying, Zhao, Hai-Li, Song, Mou-Dao, Zhang, Bang-Hua, Zhang, Bao-Long
Format: Article
Language:English
Subjects:
Acrylamides - chemistry
Adsorption
Aldehydes - chemistry
Amines - chemistry
Animals
Biocompatible Materials - chemistry
Catalytic Domain
Cattle
chitosan
Chitosan - chemistry
Hemoglobins - chemistry
Microscopy, Electron, Scanning
molecular imprinting
Polymers - chemistry
protein recognition
silica particles
Silicon Dioxide - chemistry
Spectroscopy, Fourier Transform Infrared
Thermogravimetry - methods
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A novel molecular imprinting method was used to prepare twice‐coated silica particles with specific recognition sites for hemoglobin. Chitosan was used as an intermedium to be coated on silica particles via phase inversion process, and the abundance of exposed amine groups (NH2) were active sites for introducing aldehyde groups. After hemoglobin was covalently immobilized by forming imine bonds with the aldehyde groups, acrylamide was then polymerized onto chitosan‐coated silica particles to form the recognition sites. The obtained hemoglobin imprinted [molecularly imprinted polymer (MIP)] beads were characterized by FTIR spectroscopy, thermogravimetric analysis (TG), and scanning electron microscopy (SEM). The MIP particles exhibited selectively adsorption for the imprinted protein compared to the nonselectively adsorption for most of proteins of the nonimprinted (NIP) beads. © 2008 Wiley Periodicals, Inc. J Biomed Mater Res, 2009
ISSN:1549-3296
1552-4965
DOI:10.1002/jbm.a.32084