Molecularly imprinted polymers (MIPs) are tailor‐made synthetic antibodies possessing specific binding cavities designed for a target molecule. Currently, MIPs for protein targets are synthesized by imprinting a short surface‐exposed fragment of the protein, called epitope or antigenic determinant. However, finding the epitope par excellence that will yield a peptide “synthetic antibody” cross‐reacting exclusively with the protein from which it is derived, is not easy. We propose a computer‐based rational approach to unambiguously identify the “best” epitope candidate. Then, using Saturation Transfer Difference (STD) and WaterLOGSY NMR spectroscopies, we prove the existence of specific binding sites created by the imprinting of this peptide epitope in the MIP nanogel. The optimized MIP nanogel could bind the epitope and cognate protein with a high affinity and selectivity. The study was performed on Hepatitis A Virus Cell Receptor‐1 protein, also known as KIM‐1 and TIM‐1, for its ubiquitous implication in numerous pathologies.

Molecularly imprinted polymers (MIPs) are chemical antibody mimics obtained by nanomoulding the 3D shape and chemical functionalities of a desired target in a synthetic polymer. Consequently, they possess exquisite molecular recognition cavities for binding the target molecule, often with specificity and affinity similar to those of antigen‐antibody interactions. Research on MIPs targeting proteins began in the mid‐90s, and this review will evaluate the progress made till now, starting from their synthesis in a monolith bulk format through surface imprinting to biocompatible soluble nanogels prepared by solid‐phase synthesis. MIPs in the latter format will be discussed more in detail because of their tremendous potential of replacing antibodies in the biomedical domain like in diagnostics and therapeutics, where the workforce of antibodies is concentrated. Emphasis is also put on the development of epitope imprinting, which consists of imprinting a short surface‐exposed fragment of a protein, resulting in MIPs capable of selectively recognizing the whole macromolecule, amidst others in complex biological media, on cells or tissues. Thus selecting the ‘best’ peptide antigen is crucial and in this context a rational approach, inspired from that used to predict peptide immunogens for peptide antibodies, is described for its unambiguous identification.

Molecularly imprinted polymers (MIPs), often dubbed "synthetic antibodies", can recognize and bind their target molecule with high affinity and selectivity, making them serious competitors with regard to biological antibodies. MIPs have gained popularity in various clinical applications and have even been applied in vivo. However, only a few studies on the biocompatibility of MIPs have been reported. Herein, we investigate on an example of a MIP that has proved its efficacy as an active agent to suppress body odors in cosmetic formulations, its effect on the viability and irritation potential of human epithelial cells. Since body odors are caused by bacteria present on the skin, bactericides are regularly added to deodorants sold on the market. However, there is growing anxiety concerning these bactericides as they can generate resistant bacteria, a problem for human and animal health. Therefore, we also assessed whether the MIP perturbs the resident skin bacteria, which were isolated from human sweat. Our results show that MIPs do not affect bacterial growth when cultured in liquid media, suggesting that they will not affect the skin flora, which protects the body from dangerous pathogens. This thorough in vitro toxicological assessment shows the biocompatibility of MIPs and constitutes a step further in their future consideration within cosmetic or pharmaceutical formulations for skin applications.

Cadherins are cell-surface proteins that mediate cell-cell adhesion. By regulating their grip formation and strengh, cadherins play a pivotal role during normal tissue morphogenesis and homeostasis of multicellular organisms. However,...