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Preparation and Characterization of Nanoliposomes for the Entrapment of Bioactive Hydrophilic Globular Proteins

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Published on: August 31, 2019

Characterization of 10MAG/LDAO reverse micelles: Understanding versatility for protein encapsulation.

Crystal I Stackhouse¹, Kali N Pierson¹, Courtney L Labrecque²

¹Department of Physics and Astronomy, Rowan University, 201 Mullica Hill Rd, Glassboro, NJ 08028, United States; Department of Biomedical and Biological Sciences, Rowan University, 201 Mullica Hill Rd, Glassboro, NJ 08028, United States.

Biophysical Chemistry

|May 30, 2024

Summary

This study reveals that 1-decanoyl-rac-glycerol (10MAG) and lauryldimethylamine-N-oxide (LDAO) reverse micelles (RMs) form oblate ellipsoids, not spheres. Proteins influence RM size, enabling tailored nanoscale encapsulation for biophysical studies.

Keywords:

1-decanoyl-rac-glycerol 10MAG/LDAO Dynamic light scattering Lauryldimethylamine-N-oxide NMR spectroscopy Reverse micelle Small angle x-ray scattering

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Area of Science:

Biophysics
Supramolecular Chemistry
Nanotechnology

Background:

Reverse micelles (RMs) are crucial nanostructures for encapsulating biomolecules in biophysical studies.
Traditional RM models assume spherical, monodisperse populations, which may not reflect complex biological systems.
The 1-decanoyl-rac-glycerol (10MAG) and lauryldimethylamine-N-oxide (LDAO) surfactant system exhibits unique protein stability within RMs.

Purpose of the Study:

To investigate the distinct structural and thermodynamic properties of 10MAG/LDAO RMs.
To characterize how protein encapsulation influences RM behavior and water loading.
To explore the potential of 10MAG/LDAO RMs for nanoscale confinement studies.

Main Methods:

Encapsulation of model proteins (cytochrome c, myoglobin, flavodoxin) in 10MAG/LDAO RMs.
Utilizing various experimental techniques for system characterization.
Analyzing the impact of water loading (W0) on RM morphology and size distribution.

Main Results:

10MAG/LDAO RMs adopt oblate ellipsoidal shapes, deviating from the spherical model.
Increased water loading leads to more numerous, spherical ellipsoidal RMs with bulk-like water pools.
Encapsulated proteins dictate optimal RM size, influencing the size of protein-free RMs.

Conclusions:

The 10MAG/LDAO system offers a unique, malleable platform for nanoscale encapsulation.
Findings challenge traditional RM models and highlight protein-specific thermodynamic influences.
This research provides a foundation for applying 10MAG/LDAO RMs in biological and chemical nanoscale confinement analyses.