Investigating the mechanism of protein surface imprinting through miniemulsion polymerisation

Abstract

Molecular imprinting is a well-established technique to create synthetic binding sites on a polymer matrix. Traditionally, this technique has been widely used to create synthetic receptors for smaller molecules but limited success has been achieved for larger molecules such as proteins. In this work, we have synthesised protein-imprinted nanoparticles using miniemulsion polymerisation, with methyl methacrylate and ethylene glycol dimethacrylate as the functional and cross-linking monomers, respectively. Initially, Ribonuclease A was chosen as the template protein and the nanoparticles showed high molecular selectivity for the protein. However, when bovine serum albumin or lysozyme was used as the template, molecular recognition was not successfully achieved. The latter part of the work was focused on understanding the mechanism involved during the imprinting in order to explain why molecular imprinting was achieved with varying success depending on the template protein.