An array of 4000 defined and addressable tripeptides
on a polymer-coated
glass slide is used to synthesize molecularly imprinted polymer (MIP)
nanoparticles. This work is undertaken to systematically probe the
impact of the peptide sequence on the ability to generate affinity
MIPs. The polymer affinity is assessed by measuring the fluorescence
of bound MIP nanoparticles at each peptide spot on the surface after
washing the array to remove any low-affinity polymer. The generic
composition commonly used in the preparation of MIPs against proteins
seems to be equally suitable for imprinting hydrophobic and hydrophilic
tripeptides. The amino acids frequently contributing to the formation
of high-affinity MIPs include T, F, D, N, Y, W, and P. The amino acids
that rarely contribute to the formation of high-affinity interactions
with MIPs are G, V, A, L, I, and M. These observations are confirmed
by computational modeling. The basic technique proposed here may be
applicable in optimizing polymer compositions for the production of
high-affinity MIPs or, more specifically, for the selection of appropriate
amino acid sequences when peptide epitopes are used instead of whole
protein imprinting.
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