Heat-Induced Structural Changes in Lactoferrin for Enhanced Mucoadhesion.

ABSTRACT: The development of biocompatible and safe mucoadhesive materials is critical for improving therapeutic strategies, where cationic proteins such as lactoferrin are emerging as promising alternatives to synthetic polymers. Here, we demonstrate how thermal denaturation of lactoferrin can be used as a viable strategy to enhance mucoadhesion. We identify and study in detail the structural changes in lactoferrin upon thermal denaturation using light scattering, circular dichroism spectroscopy, gel-electrophoresis, and atomic force microscopy. Lactoferrin-mucin binding was evaluated using rheology, confocal microscopy, and quartz crystal microbalance with dissipation monitoring. We find that lactoferrin binds to mucin at its native state, heat-treatment at 95 °C enhances its affinity for mucin, a

SUBMITTER: Hazt B 

PROVIDER: S-EPMC12628292 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature