Since their conception fifty years ago, molecularly imprinted polymers (MIPs) have seen extensive development both in terms of synthetic routes and applications. Perhaps the most challenging target for molecular imprinting are cells. Though early work was based almost entirely around microprinting methods, recent developments shifted towards epitope imprinting to generate MIP nanoparticles. Simultaneously, the development of techniques such as solid phase MIP synthesis have solved many historic issues of MIP production. This review briefly describes various approached used in cell imprinting with a focus on applications of the created materials in imaging, drug delivery, diagnostics and tissue engineering.
A novel abiotic assay based on biotin-specific fluorescent molecularly imprinted polymer nanoparticles (nanoMIPs) which acted as both reporter probes and binding agents, was developed. This is a first report of an assay which, unlike ELISA, required no washing steps or addition of enzyme substrates, making it more user-friendly. The components of the molecularly imprinted polymer nanoparticles assay (MINA) were assembled in microtiter plates fitted with magnetic inserts. The fluorescent nanoMIPs were bound to biotin-conjugated magnetic particles, which were attracted to the inserts. The addition of free biotin caused a displacement of the fluorescent nanoMIPs into solution, generating a signal proportional to the concentration of biotin. The nanoMIPs had a dissociation constant (Kd) of 14 nM, allowing the assay to detect biotin at nano-molar concentrations. The preassembled assay only required the addition of the sample and measurement of the fluorescence, and it functioned well after six weeks of storage without refrigeration. The assay did not show the susceptibility to several compounds which are known to interfere with avidin and streptavidin-based assays, such as mercaptoethanol and sugars. The protocols optimized in this work could be used to develop the abiotic assays for any other compound of interest.[a] S.
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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