Nowadays, pharmaceutical companies are facing several challenges with the development and approval of new biological products. The unique properties of several fluorinated ionic liquids (FILs), such as their high surfactant power in aqueous solutions, their chemical and biological stability, and low toxicity, favor their application in the pharmaceutical industry. Furthermore, the numerous combinations between cations and anions, in the FILs design, enlarge the possibilities to construct a successful delivery system. Several FILs also proved to not affect the activity, stability, and secondary structure of the therapeutic protein lysozyme. This work aims to study the aggregation behavior of distinct FILs in the protein suitable medium, in the presence or absence of lysozyme. Besides, different incubation conditions were tested to guarantee the optimal enzymatic activity of the protein at more stable delivery systems. Following the optimization of the incubation conditions, the quantification of the encapsulated lysozyme was performed to evaluate the encapsulation efficiency of each FIL-based system. The release of the protein was tested applying variables such as time, temperature, and ultrasound frequency. The experimental results suggest that the aggregation behavior of FILs is not significantly influenced by the protein and/or protein buffer and supports their application for the design of delivery systems with high encapsulation efficiencies, maintaining the biological activity of either encapsulated and released protein.
Keywords: aggregation behavior; biological activity; delivery systems; encapsulation efficiency; fluorinated ionic liquids; release.