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Heat-Induced Structural Changes in Lactoferrin for Enhanced Mucoadhesion
Bianca Hazt1, Daniel J Read2, Oliver G Harlen2
1Food Colloids and Bioprocessing Group, School of Food Science and Nutrition, University of Leeds, Leeds LS2 9JT, U.K.
ACS Applied Bio Materials
|October 18, 2025
Summary
Heating lactoferrin (a protein) enhances its mucoadhesion by altering its structure. This protein-based mucoadhesion relies on hydrophobic interactions, offering a new strategy for drug delivery systems.
Area of Science:
- Biomaterials Science
- Protein Engineering
- Drug Delivery Systems
Background:
- Biocompatible mucoadhesive materials are crucial for effective therapeutic strategies.
- Cationic proteins like lactoferrin show promise as natural alternatives to synthetic mucoadhesives.
Purpose of the Study:
- To investigate thermal denaturation of lactoferrin as a method to enhance mucoadhesion.
- To elucidate the structural changes and binding mechanisms involved in lactoferrin-mucin interactions.
Main Methods:
- Structural analysis using light scattering, circular dichroism spectroscopy, gel-electrophoresis, and atomic force microscopy.
- Mucoadhesion evaluation via rheology, confocal microscopy, and quartz crystal microbalance with dissipation monitoring.
Main Results:
- Heat treatment (95 °C) significantly enhances lactoferrin's affinity for mucin.
- The enhanced mucoadhesion mechanism is primarily driven by hydrophobic interactions, not disulfide bonds.
- Lactoferrin-mucin complexes exhibit high surface activity and artificial shear-thinning properties.
Conclusions:
- Thermal denaturation is a viable strategy to improve lactoferrin-based mucoadhesion.
- Hydrophobic interactions play a key role in the enhanced mucoadhesion of denatured lactoferrin.
- This study provides a novel design approach for developing advanced natural protein-based mucoadhesive systems.
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