Synthesis of polyacrylamide gel beads with electrostatic functional groups for the molecular imprinting of bovine serum albumin

Abstract

Synthetic materials capable of recognizing proteins are important in separation, biosensors and biomaterials. In this study, bovine serum albumin-imprinted soft-wet polyacrylamide gel beads were prepared via inverse-phase suspension polymerization, using acrylamide and N,N'-methylene diacrylamide as polymeric matrix components and methacrylic acid as functional monomer. The adsorption study showed, through the imprinting process, that the imprinted gel beads had much higher adsorption capacity than the nonimprinted gel beads, and that the matching of the surface zeta-potential between the templates and the imprinted gel beads can enhance the imprinting effect. Adsorption kinetics indicated that the adsorption process could be described as an apparent first-order kinetic process for the gel beads. From the adsorption isotherm curve, we found that the adsorption of the imprinted gel beads was in agreement with the Langmuir adsorption model. Moreover, selectivity testing of the imprinted gel beads showed that imprinted gel beads exhibited good recognition for BSA as compared to the control protein. We speculate that the formation of complementary shapes and multiple-point electrostatic interactions between the imprinting cavities and the template proteins are the two factors that lead to the imprinting effect.

From 3D to 2D: A Review of the Molecular Imprinting of Proteins

“…In turn, this porosity weakens the structure of any polymer, leading to stability and practical issues. In general, bulk acrylate materials imprinted for proteins tend to rely on loose-linked polymers with specific sites embedded in them (49,(51)(52)(53)67). This low cross-linking affords reasonable mass transfer and, as demonstrated with hydrogels, can offer swelling as an additional factor for template removal and rebinding.…”

“…This low cross-linking affords reasonable mass transfer and, as demonstrated with hydrogels, can offer swelling as an additional factor for template removal and rebinding. The ability to control pore size by environmental conditions is of great benefit, as demonstrated clearly in the acrylate beads developed by Pang, which showed clear macroporous structure (67) at the working range of his protocol. The advent of hydrogel technology has brought the possibility of combining protein encapsulation and specific imprinting.…”

“…Methacrylic acid based gel beads were imprinted with bovine serum albumin (BSA) by Pang, using an inverse-phase suspension method (67). They obtained good quality spherical beads exhibiting excellent macroporous structure, which is important in facilitating the movement of proteins through the material.…”

Electrochemical biosensor based on biomimetic material for myoglobin detection

“…Furthermore, the great flexibility of the protein structure means that it should be polymerized under almost-native conditions so that its shape would be preserved and the binding site accurately designed. Acrylamide matrices meet these criteria [35][36][37][38]. They polymerize under mild conditions and carry uncharged functions that establish hydrogen bonds and dipole-dipole interactions with Myo [6].…”

Transferrin recognition based on a protein imprinted material prepared by hierarchical imprinting technique

“…In the former case [16,20,21], the binding sites are formed throughout bulk materials, originated from small molecule imprinting, but suffered from poor mass transfer and heterogeneity of recognition sites [22]. In the latter case, binding sites are formed on the material surface [22,23], which gains the popularity because of easy recognition accessibility and template removal.…”