Please use this identifier to cite or link to this item: https://doi.org/10.1021/ac061364y
Title: Preparation of superparamagnetic ribonuclease A surface-imprinted submicrometer particles for protein recognition in aqueous media
Authors: Tan, C.J.
Tong, Y.W. 
Issue Date: 1-Jan-2007
Citation: Tan, C.J., Tong, Y.W. (2007-01-01). Preparation of superparamagnetic ribonuclease A surface-imprinted submicrometer particles for protein recognition in aqueous media. Analytical Chemistry 79 (1) : 299-306. ScholarBank@NUS Repository. https://doi.org/10.1021/ac061364y
Abstract: Superparamagnetic ribonuclease A surface-imprinted polymeric particles that can preferentially bind the template protein in an aqueous environment were prepared in this study. Methyl methacrylate and ethylene glycol dimethacrylate were employed as the functional and cross-linker monomers, respectively. Regularly shaped submicrometer (700-800 nm) particles imprinted with ribonuclease A were successfully prepared using redox-initiated mini-emulsion polymerization. Nanosized Fe3O4 magnetite was encapsulated in the imprinted particles with good encapsulation efficiency (17.5 wt %) for the incorporation of the superparamagnetic property. Good selectivity toward the template over the control protein in an aqueous environment was demonstrated by the imprinted particles in the batchwise and competitive rebinding tests with the highest template loading, Qmax, of 127.7 mg/g observed in the batch rebinding test Given the small sizes of the imprinted particles and the presence of the binding sites on the surface, the rebinding process was kinetically favorable despite the sheer bulk of the macromolecules. In the desorption study, it was found that the more hydrophobic solvent was more effective for ribonuclease A desorption from the imprinted particles. This indicated that the hydrophobic effect was probably the main form of interaction responsible for the template rebinding to the imprinted sites in an aqueous media. © 2007 American Chemical Society.
Source Title: Analytical Chemistry
URI: http://scholarbank.nus.edu.sg/handle/10635/89925
ISSN: 00032700
DOI: 10.1021/ac061364y
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

124
checked on Sep 17, 2018

WEB OF SCIENCETM
Citations

114
checked on Sep 17, 2018

Page view(s)

29
checked on Aug 3, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.