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Abstract: A molecularly imprinted film was fabricated, in the presence of epitope-peptides, onto a quartz crystal microbalance (QCM) chip. These five peptides are known linear or conformational epitopes of the anthrax protective antigen PA83. Imprinting resulted in an epitope-cavity with affinity for the corresponding template. With the use of a basic monomer, the binding-effect was further enhanced increasing the affinity to nanomolar levels. The affinities of the peptide to their corresponding molecularly induced polymers (MIPs) were more closely related to the molecular weight of the analyte than to the number of residues. All epitope-cavities differentiated their epitope region on the protective antigen PA83 as well as the corresponding furin cleavage fragments PA63 and PA20. The QCM chip differential response to the protective antigen fragment was observed in the picomolar range, thus demonstrating a method to manipulate protein on the surface with defined orientation
Template and target information: peptides, protein epitopes, anthrax protective antigen, PA83, PA63, PA20, VKKSDEYTF, RYDMLNISSLRQDG, YNDKLPLYISNPNY, DKLPLYISNPNY, NGDTSTNGIK