Pharmaceutica Analytica Acta

Abstract

Molecularly imprinted polymer nanostructure for drug stability and binding affinities in biotherapeutics

Roongnapa Suedee*, Watchara Pholthien, Krit Prakannoppaku, Nanticha Kaewsud, Khanittha Santipiboon and Pimpisut Getsuvan

Molecularly Imprinted Polymers (MIPs) are transforming our understanding of protein interactions in the (bio) pharmaceutical arena. These innovative materials are instrumental in developing therapies, optimizing drug delivery, and enhancing diagnostics by enabling effective evaluation of binding affinities. Protein nanocapsules that reassemble at room temperature offer remarkable flexibility. However, fine-tuning their surface remains cutting-edge. These interactions are crucial to unlocking the full potential of Cannabidiol (CBD), particularly in its antioxidant and immunostimulatory roles when interacting with proteins such as human serum albumin. By employing selective membranes, we can precisely identify liquid proteins and uncover epitope variations influenced by excipient density and buffer composition, which significantly impact nanofibril anchoring. Accurate detection of epitopes is essential for lipid and sterol biosynthesis, but variations in the medium can affect protein stability and binding affinity. Additionally, the technique used for drug blending plays a vital role in stability. Utilizing dispersive mechanisms can enhance sustained drug release and further stabilize proteins, thereby improving cellular exposure. Our data demonstrate that CBD levels have no effect on MIP structure or enzyme activity, as confirmed by advanced techniques such as X-ray mapping and Field-Emission Scanning Electron Microscopy (FESEM). High-resolution Fouriertransform Infrared (FT-IR) analyses indicate that stabilized Polycaprolactone-Triol (PCL-T) hydrogels promote drug clustering and cell interactions. Moreover, MIPs can mimic natural antibodies by targeting specific markers to deliver epitopes, such as anti-IgE, effectively reducing allergy symptoms. Cuttingedge methods such as Liquid Chromatography coupled with Mass Spectrometry (LC-QTOF-MS) reveal the distinct arrangements of charged residues in proteins, which influence stability and interactions. Additionally, immunoaffinity capture reveals that stable charge states within the PCL-T hydrogel engage with albumin during pH shifts. These dynamic advancements not only enhance the stability and antioxidant properties of CBD but also improve the functionality of larger membrane protein sites created through imprinting. The efficiency of cysteinerich regions facilitates insightful studies into CBD’s role in inhibiting cellular processes. The remarkable potential of cannabinoids extends beyond reducing inflammation to boosting antimicrobial effects. Using innovative techniques such as Scanning Electron Microscopy (SEM) and fluorescence laser microscopy, we discovered intriguing proteinprotein interactions in both solvent and non-solvent environments. Our findings on pH- and cholate-anchored Molecularly Imprinted Polymers (MIPs) showcase the dynamic nature of nanocapsules, which significantly influence drug degradation and amino acid absorption. Moreover, variations in nanoparticle and protein mobility highlight the essential role of Adenosine Triphosphate (ATP) in the behavior of antibodies and insulin’s binding to Human Serum Albumin (HSA). This research makes a meaningful contribution to biopharmaceutical science, delving deep into biomolecule concentrations, protein folding, and cutting-edge imaging techniques. We’re excited to introduce blue-light-responsive photoswitches, which demonstrate how nanocapsule size can impact hydrogel stability and ion interactions at the protein-hydrogel interface. The correlation between weight loss at melting temperatures and aggregation in water-hydrated Immunoglobulin G (IgG) during freeze-drying is noteworthy. Our Nuclear Magnetic Resonance spectroscopy (NMR) studies link biomolecular concentration to protein folding, thereby enhancing the efficiency of antibodies and enzymes. In conclusion, these findings reveal the potential of cannabinoids to improve stability and prevent protein aggregation, paving the way for innovative bioprocess and formulation development. Nuclear Magnetic Resonance (NMR) insights also suggest that lipid bilayers containing thermoresponsive proteins behave as hybrid materials, thereby optimizing drug delivery

Published Date: 2026-06-24; Received Date: 2026-05-25