4.7 Article

Disclosing the Potential of Fluorinated Ionic Liquids as Interferon-Alpha 2b Delivery Systems

Journal

NANOMATERIALS
Volume 12, Issue 11, Pages -

Publisher

MDPI
DOI: 10.3390/nano12111851

Keywords

therapeutic proteins; ionic liquids; aggregation behaviour; interactions; delivery systems

Funding

  1. FCT/MCTES (Portugal) [SFRH/BD/130965/2017, COVID/BD/151919/2021]
  2. Associate Laboratory for Green ChemistryLAQV - FCT/MCTES [UIDB/50006/2020|UIDP/50006/2020]
  3. [2020.00835.CEECIND/2021.01432.CEECIND]
  4. [PTDC/EQUEQU/2223/2021]
  5. Fundação para a Ciência e a Tecnologia [SFRH/BD/130965/2017, COVID/BD/151919/2021] Funding Source: FCT

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This study investigates the influence of IFN-alpha 2b on the aggregation behavior of fluorinated ionic liquids (FILs) and the interactions between them. The results show that the presence of IFN-alpha 2b affects the aggregation behavior of FILs and strong interaction occurs between them. FILs can be tailored to carry IFN-alpha 2b and prevent protein aggregation through the formation of a conjugate.
Interferon-alpha 2b (IFN-alpha 2b) is a therapeutic protein used for the treatment of cancer, viral infections, and auto-immune diseases. Its application is hindered by a low bioavailability and instability in the bloodstream, and the search for new strategies for a target delivery and stabilization of IFN-alpha 2b to improve its therapeutic efficacy is crucial. Fluorinated ionic liquids (FILs) are promising biomaterials that: (i) can form self-assembled structures; (ii) have complete miscibility in water; and (iii) can be designed to have reduced toxicity. The influence of IFN-alpha 2b in the aggregation behaviour of FILs and the interactions between them were investigated through conductivity and surface tension measurements, and using electron microscopic and spectroscopy techniques to study FILs feasibility as an interferon-alpha 2b delivery system. The results show that the presence of IFN-alpha 2b influences the aggregation behaviour of FILs and that strong interaction between the two compounds occurs. The protein might not be fully encapsulated by FILs. However, the FIL can be tailored in the future to carry IFN-alpha 2b by the formation of a conjugate, which prevents the aggregation of this protein. This work constitutes a first step toward the design and development of FIL-based IFN-alpha 2b delivery systems.

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