A thalidomide templated molecularly imprinted polymer that promotes a biologically active chiral entity tagged in colon carcinoma cells and protein-related immune activation

• Study of MIPs that can promote cellular uptake of colon carcinoma cells and protein assemblies.
• Two distinctly different patterns for the enantiomorphs of thalidomide have been identified.
• An almost equimolar ratio of two crosslinkers prolonged better the release of the R-enantiomer.
• The QD-embedded MIP revealed the disassembly complex of a faded dot in the twin proteins.
• The adsorbed surface of a MIP is crucial for stereochemistry tagged for biological function.

Molecularly imprinted polymers (MIP) with selective layered surface were utilized for the potential allowing the original molecule to be tagged as a biologically active chiral entity in a biological cancer milieu. The general features of the particles consisted of different monomeric compositions for the copolymerization deposited on the surfaces. We found that the addition of an almost equimolar ratio of two crosslinkers enabled thalidomide to be bound 70% and prolonged release of the R-form to a greater extent than that achieved using a single crosslinker. The effect of the altered surface on the ability of the enantiomers and racemic thalidomide to cross a lipid bilayer and the optical properties of a quantum dot has been studied. These chirally imprints provided the controlled interfacial interactions at the self-assembly site, coupled to the electronic reactions, related to probing the recognition events in the apoptosis cancer cells. This result revealed the three-dimensional fluorescence imaging for evaluation drug release that give rise a much greater decrease of cell viability of the Caco-2 cells. Furthermore, the increased hydrophobicity on the surface enhanced fluorescence due to an effective complex with three-dimensional shape of the active site inside the cavity. Evidently, the endogenous components affected the interacting of the albumin capable of the activation of immune system on the cell allowed discriminating a form of thalidomide. The results indicated that the thalidomide-tagged protein on enantiomorphs selective-MIPs optimising its cancer delivery application, yet promoted the identification of target-ligand interactions for pharmaceutical effect and the toxicities of thalidomide enantiomers.

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