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Orientational Transition in a Liquid Crystal Triggered by the Thermodynamic Growth of Interfacial Wetting Sheets

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Lysozyme entrapped within reverse hexagonal mesophases: physical properties and structural behavior.

Tehila Mishraki¹, Dima Libster, Abraham Aserin

¹Casali Institute of Applied Chemistry, The Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem 91904, Israel.

Colloids and Surfaces. B, Biointerfaces

|September 15, 2009

Summary

Incorporating lysozyme into hexagonal phases enhances protein stability and alters material properties through strong hydrogen bonding interactions between the protein and surfactant. This demonstrates hexagonal systems

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Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases

Published on: November 21, 2010

Area of Science:

Materials Science
Biophysics
Physical Chemistry

Background:

Lysozyme (LSZ) is a model protein.
Monoolein-based reverse hexagonal (H(II)) mesophases are self-assembled lipid structures.
Understanding protein-lipid interactions is crucial for biomaterial development.

Purpose of the Study:

To investigate the structural effects of incorporating lysozyme into monoolein-based H(II) mesophases.
To clarify modifications in H(II) mesophase organization and lysozyme conformational stability.
To explore the potential of hexagonal systems as protein carriers.

Main Methods:

Small-angle X-ray scattering (SAXS) for structural analysis.
Attenuated total reflection Fourier-transform infrared (ATR-FTIR) spectroscopy for molecular interactions.
Rheological measurements to assess mechanical properties.

Main Results:

Lysozyme (up to 3 wt.%) was successfully solubilized, forming strong hydrogen bonds with glycerol monooleate (GMO) and causing minor lattice parameter decrease.
Lysozyme alpha-helix conformation was stabilized at high pH, and the H(II) phase reduced unfavorable alpha-->beta transitions, enhancing protein stability against denaturation.
Incorporation of lysozyme increased the elastic properties and solid-like response of the hexagonal structures due to enhanced interfacial hydrogen bonding.

Conclusions:

Monoolein-based hexagonal phases can effectively incorporate and stabilize proteins like lysozyme.
The observed molecular interactions and structural changes enhance protein conformational stability and modify the rheological properties of the mesophases.
These findings highlight the potential of hexagonal systems for protein delivery and stabilization in various applications.