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Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids

Proteins are inherently unstable, which limits their use as therapeutic agents. However, the use of biocompatible cosolvents or surfactants can help to circumvent this problem through the stabilization of intramolecular and solvent-mediated interactions. Ionic liquids (ILs) have been known to act as...

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Autores principales: Alves, Márcia M. S., Melo, Manuel N., Mertens, Haydyn D. T., Pereiro, Ana B., Archer, Margarida
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9863861/
https://www.ncbi.nlm.nih.gov/pubmed/36678790
http://dx.doi.org/10.3390/pharmaceutics15010157
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author Alves, Márcia M. S.
Melo, Manuel N.
Mertens, Haydyn D. T.
Pereiro, Ana B.
Archer, Margarida
author_facet Alves, Márcia M. S.
Melo, Manuel N.
Mertens, Haydyn D. T.
Pereiro, Ana B.
Archer, Margarida
author_sort Alves, Márcia M. S.
collection PubMed
description Proteins are inherently unstable, which limits their use as therapeutic agents. However, the use of biocompatible cosolvents or surfactants can help to circumvent this problem through the stabilization of intramolecular and solvent-mediated interactions. Ionic liquids (ILs) have been known to act as cosolvents or surface-active compounds. In the presence of proteins, ILs can have a beneficial effect on their refolding, shelf life, stability, and enzymatic activities. In the work described herein, we used small-angle X-ray scattering (SAXS) to monitor the aggregation of different concentrations of ILs with protein models, lysozyme (Lys) and bovine serum albumin (BSA), and fluorescence microscopy to assess micelle formation of fluorinated ILs (FILs) with Lys. Furthermore, coarse-grained molecular dynamics (CG-MD) simulations provided a better understanding of Lys–FIL interactions. The results showed that the proteins maintain their globular structures in the presence of FILs, with signs of partial unfolding for Lys and compaction for BSA with increased flexibility at higher FIL concentrations. Lys was encapsulated by FIL, thus reinforcing the potential of ILs to be used in the formulation of protein-based pharmaceuticals.
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spelling pubmed-98638612023-01-22 Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids Alves, Márcia M. S. Melo, Manuel N. Mertens, Haydyn D. T. Pereiro, Ana B. Archer, Margarida Pharmaceutics Article Proteins are inherently unstable, which limits their use as therapeutic agents. However, the use of biocompatible cosolvents or surfactants can help to circumvent this problem through the stabilization of intramolecular and solvent-mediated interactions. Ionic liquids (ILs) have been known to act as cosolvents or surface-active compounds. In the presence of proteins, ILs can have a beneficial effect on their refolding, shelf life, stability, and enzymatic activities. In the work described herein, we used small-angle X-ray scattering (SAXS) to monitor the aggregation of different concentrations of ILs with protein models, lysozyme (Lys) and bovine serum albumin (BSA), and fluorescence microscopy to assess micelle formation of fluorinated ILs (FILs) with Lys. Furthermore, coarse-grained molecular dynamics (CG-MD) simulations provided a better understanding of Lys–FIL interactions. The results showed that the proteins maintain their globular structures in the presence of FILs, with signs of partial unfolding for Lys and compaction for BSA with increased flexibility at higher FIL concentrations. Lys was encapsulated by FIL, thus reinforcing the potential of ILs to be used in the formulation of protein-based pharmaceuticals. MDPI 2023-01-03 /pmc/articles/PMC9863861/ /pubmed/36678790 http://dx.doi.org/10.3390/pharmaceutics15010157 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Alves, Márcia M. S.
Melo, Manuel N.
Mertens, Haydyn D. T.
Pereiro, Ana B.
Archer, Margarida
Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids
title Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids
title_full Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids
title_fullStr Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids
title_full_unstemmed Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids
title_short Studies on the Interaction between Model Proteins and Fluorinated Ionic Liquids
title_sort studies on the interaction between model proteins and fluorinated ionic liquids
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9863861/
https://www.ncbi.nlm.nih.gov/pubmed/36678790
http://dx.doi.org/10.3390/pharmaceutics15010157
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