MIPs and Aptamers for Recognition of Proteins in Biomimetic Sensing

Marcus Menger, Aysu Yarman, Júlia Erdőssy, Huseyin Yildiz, Róbert Gyurcsányi, Frieder Scheller
2016 Biosensors  
Biomimetic binders and catalysts have been generated in order to substitute the biological pendants in separation techniques and bioanalysis. The two major approaches use either "evolution in the test tube" of nucleotides for the preparation of aptamers or total chemical synthesis for molecularly imprinted polymers (MIPs). The reproducible production of aptamers is a clear advantage, whilst the preparation of MIPs typically leads to a population of polymers with different binding sites. The
more » ... ization of binding sites in the total bulk of the MIPs results in a higher binding capacity, however, on the expense of the accessibility and exchange rate. Furthermore, the readout of the bound analyte is easier for aptamers since the integration of signal generating labels is well established. On the other hand, the overall negative charge of the nucleotides makes aptamers prone to non-specific adsorption of positively charged constituents of the sample and the "biological" degradation of non-modified aptamers and ionic strength-dependent changes of conformation may be challenging in some application. of proteins. A broad spectrum of "selective sorbents" and later of synthetic polymers with specific binding sites-so called molecularly imprinted polymers (MIPs)-has been developed based on early concepts from the 1930s [1,2] and 1940s [3] (Figure 1 ). This involves polymerizing functional monomers in the presence of a target compound (analyte for analytical applications) to result in synthetic polymers that bear the imprint of the target, i.e., the imprinting process generates binding sites for a given target. The prerequisite of a successful molecular imprinting is the interaction of the target through covalent (pre-organized approach) [4,5] or non-covalent (self-assembly approach) [6] [7] [8] bonds with the chemically active moieties of the functional monomers in the pre-polymerization mixture. This arrangement is fixed in the subsequent polymerization of the functional monomers and reaction with a cross-linker. After polymerization, the template molecules are removed, providing binding sites that are ideally complementary in size, shape and functionality to the template, thus, the template preferentially rebinds to these sites. Biosensors 2016, 6, 35 2 of 18 selective recognition of proteins. A broad spectrum of "selective sorbents" and later of synthetic polymers with specific binding sites-so called molecularly imprinted polymers (MIPs)-has been developed based on early concepts from the 1930s [1,2] and 1940s [3] (Figure 1 ). This involves polymerizing functional monomers in the presence of a target compound (analyte for analytical applications) to result in synthetic polymers that bear the imprint of the target, i.e., the imprinting process generates binding sites for a given target. The prerequisite of a successful molecular imprinting is the interaction of the target through covalent (pre-organized approach) [4,5]or non-covalent (self-assembly approach) [6-8] bonds with the chemically active moieties of the functional monomers in the pre-polymerization mixture. This arrangement is fixed in the subsequent polymerization of the functional monomers and reaction with a cross-linker. After polymerization, the template molecules are removed, providing binding sites that are ideally complementary in size, shape and functionality to the template, thus, the template preferentially rebinds to these sites.
doi:10.3390/bios6030035 pmid:27438862 pmcid:PMC5039654 fatcat:a3kd3tmrkfg2dnnxxiarfywiru