Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/90596
Title: Investigation of protein imprinting using miniemulsion polymerization through the epitope approach
Authors: Jin, T.C.
Wah, T.Y. 
Keywords: Cytochrome C
Epitope
Miniemulsion polymerization
Molecular imprinting
Nanoparticles
Protein
Ribonuclease A
Issue Date: 2007
Source: Jin, T.C.,Wah, T.Y. (2007). Investigation of protein imprinting using miniemulsion polymerization through the epitope approach. AIChE Annual Meeting, Conference Proceedings : -. ScholarBank@NUS Repository.
Abstract: Molecular imprinting is a state-of-the-art technique that can be applied for the preparation of polymeric materials with antibody-like affinity for pre-determined target molecules, thus offering an array of possible applications in the field of analytical chemistry and separation. Nevertheless, imprinting of protein macromolecules has only been met with limited success due to its incompatibility with the conventional molecular imprinting system. In this study, it was aimed to achieve successful protein imprinting through the epitope approach in a miniemulsion polymerization system. The peptide epitopes employed were obtained through direct chemical proteolytic digestion (for RNAse A) or synthesized using the solid-phase peptide synthesis (for cytochrome C). Epitope-imprinted nanoparticles (about 50 nm) were prepared. The nanoparticles were morphologically characterized through direct microscopy and nitrogen sorption method. In order to elucidate their recognition property, they were subjected to batch adsorption runs in single-protein and competitive environments. Preliminary results showed that the RNase A epitope-imprinted nanoparticles failed to exhibit the desired affinity towards the protein. The remaining characterization studies are still in progress.
Source Title: AIChE Annual Meeting, Conference Proceedings
URI: http://scholarbank.nus.edu.sg/handle/10635/90596
ISBN: 9780816910229
Appears in Collections:Staff Publications

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