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Temperature-dependent behavior of lysozyme within the reverse hexagonal mesophases (H(II))
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
|October 20, 2009
Summary
Lysozyme (LSZ) loaded into hexagonal mesophases enhances thermal stability by protecting its structure. The enzyme alters the mesophase domain size and elasticity, with complex temperature-dependent behaviors observed for both components.
Area of Science:
- Biophysics
- Materials Science
- Structural Biology
Background:
- Lysozyme (LSZ) is a crucial enzyme studied for its structural behavior.
- Reverse hexagonal (H(II)) mesophases are utilized as carrier systems.
- Understanding protein-mesophase interactions is vital for drug delivery and biomaterials.
Purpose of the Study:
- To investigate the temperature-dependent structural interactions between lysozyme (LSZ) and H(II) mesophases.
- To characterize the conformational stability of LSZ within the mesophase.
- To analyze the effects of LSZ incorporation on the mesophase structure and rheology.
Main Methods:
- Small-angle X-ray scattering (SAXS) for structural analysis.
- ATR-FTIR spectroscopy and fluorescence for conformational stability.
- Rheological measurements for viscoelastic properties.
Main Results:
- LSZ maintained its active site conformation within the H(II) mesophase.
- LSZ incorporation enhanced the thermal stability of the enzyme.
- LSZ influenced mesophase domain size and elasticity in a temperature-dependent manner.
- Hydrogen bonding between LSZ and monoolein polar heads was proposed.
Conclusions:
- The H(II) mesophase protects LSZ's structure and enhances its thermal stability.
- LSZ incorporation significantly modifies the structural and rheological properties of the mesophase.
- Temperature plays a critical role in the interplay between LSZ and the H(II) mesophase.
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