Molecularly Imprinted Polymer-Based Sensors for Protein Detection.

The accurate detection of biological substances such as proteins has always been a hot topic in scientific research. Biomimetic sensors seek to imitate sensitive and selective mechanisms of biological systems and integrate these traits into applicable sensing platforms. Molecular imprinting technology has been extensively practiced in many domains, where it can produce various molecular recognition materials with specific recognition capabilities. Molecularly imprinted polymers (MIPs), dubbed plastic antibodies, are artificial receptors with high-affinity binding sites for a particular molecule or compound. MIPs for protein recognition are expected to have high affinity via numerous interactions between polymer matrices and multiple functional groups of the target protein. This critical review briefly describes recent advances in the synthesis, characterization, and application of MIP-based sensor platforms used to detect proteins.

Inspirations of Biomimetic Affinity Ligands: A Review.

Affinity chromatography is a well-known method dependent on molecular recognition and is used to purify biomolecules by mimicking the specific interactions between the biomolecules and their substrates. Enzyme substrates, cofactors, antigens, and inhibitors are generally utilized as bioligands in affinity chromatography. However, their cost, instability, and leakage problems are the main drawbacks of these bioligands. Biomimetic affinity ligands can recognize their target molecules with high selectivity. Their cost-effectiveness and chemical and biological stabilities make these antibody analogs favorable candidates for affinity chromatography applications. Biomimetics applies to nature and aims to develop nanodevices, processes, and nanomaterials. Today, biomimetics provides a design approach to the biomimetic affinity ligands with the aid of computational methods, rational design, and other approaches to meet the requirements of the bioligands and improve the downstream process. This review highlighted the recent trends in designing biomimetic affinity ligands and summarized their binding interactions with the target molecules with computational approaches.

Binding modes of cibacron blue with albumin in affinity chromatography using docking tools.

Affinity chromatography is a standard method, which used for protein purification and separation studies due to its specificity and selectivity. There are several affinity chromatography methods, such as dye affinity, immobilized metal chelated affinity, and affinity electrophoresis. Cibacron Blue F3G-A (CBD), as a dye ligand, is one of the most used dyes among dye affinity chromatography. CBD is ideally suited for human serum albumin (HSA) separation and purification in affinity chromatography for several years. However, even though CBD has many purification applications, there is not much research focused on the interaction between CBD and HSA in molecular docking. The interactions between CBD and HSA were simulated via AutoDock molecular docking software in this study. Investigated possibilities resulted in six different conformations on different locations, which light the way to variable connectivity of CBD. Thus, it was determined that the most favorable binding is conformation 5, with its lowest binding energy, which is energetically favorable.