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Related Experiment Video

Updated: Aug 13, 2025

From Molecules to Materials: Engineering New Ionic Liquid Crystals Through Halogen Bonding

From Molecules to Materials: Engineering New Ionic Liquid Crystals Through Halogen Bonding

Published on: March 24, 2018

Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids.

Márcia M S Alves¹, Manuel N Melo¹, Haydyn D T Mertens²

¹Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa (ITQB NOVA), 2780-157 Oeiras, Portugal.

|January 21, 2023

Summary

Ionic liquids (ILs) stabilize therapeutic proteins, improving their shelf life and activity. This study shows fluorinated ILs protect protein structure and aid in pharmaceutical formulation.

Keywords:

encapsulation fluorinated ionic liquids protein surface-active ionic liquids

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Last Updated: Aug 13, 2025

From Molecules to Materials: Engineering New Ionic Liquid Crystals Through Halogen Bonding

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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions

Published on: October 21, 2016

Area of Science:

Biochemistry and Pharmaceutical Sciences
Materials Science
Computational Chemistry

Background:

Protein instability limits therapeutic applications.
Biocompatible cosolvents and surfactants can enhance protein stability.
Ionic liquids (ILs) show potential as stabilizing agents for proteins.

Purpose of the Study:

To investigate the stabilizing effects of fluorinated ionic liquids (FILs) on protein models.
To explore the interaction mechanisms between FILs and proteins.
To assess the potential of FILs in protein-based pharmaceutical formulations.

Main Methods:

Small-angle X-ray scattering (SAXS) to monitor protein aggregation with varying IL concentrations.
Fluorescence microscopy to assess micelle formation of FILs with lysozyme (Lys).
Coarse-grained molecular dynamics (CG-MD) simulations to understand Lys-FIL interactions.

Main Results:

Proteins (lysozyme and bovine serum albumin) maintained globular structures in the presence of FILs.
Partial unfolding of Lys and compaction of BSA were observed at higher FIL concentrations.
Encapsulation of Lys by FIL was confirmed, indicating FILs can protect protein structure.

Conclusions:

Fluorinated ionic liquids demonstrate significant potential for stabilizing therapeutic proteins.
FILs can modulate protein structure and flexibility, enhancing shelf life and activity.
These findings support the use of ILs in developing advanced protein-based pharmaceuticals.