I'm working on magnetic molecular imprinting of proteins with chitosan and sodium alginate. At the first step, I coat the fe3o4 nanoparticles with sodium alginate and then coat the result with chitosan and protein. Then, I remove the protein to make MIPs. The problem is that the MIPs absorb both specific imprinted protein (albumin) and nonspecific protein (lysozyme). Does anyone know the reason or a certain method for this kind of imprinting?
I suggest tuning the cation/anion ratio and addition of hydrophobic and charged monomers to the system.
c.f.
Article Synthesis of lysozyme imprinted column with macroporous stru...
Article Effect of Electrostatic Functional Monomers on Lysozyme Reco...
Ali Nematollahzadeh thank you so much for your advises and useful articles but i could not understand what you said about cation/anion ratio. did you mean the tuning of pH?
By cation/anion ratio I meant the ratio of chitosan (cation)/alginate (anion).
Ali Nematollahzadeh thanks for your prompt reply!! do you think that the molecular weight of chitosan can affect the results?
Hi Ali
I think that the concentration of the solution can effect on the results.
Usually monomers with large size are chosen for high molecular weight templates. Chitosan and alginate are large enough, so I think in this case the molecular size or weight wouldn't affect the imprinting performance.
Hi Rasha Shakir Nima
I would say, the concentration can affect the adsorption amount or adsorption capacity, but not the selectively so much.
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