期刊
FOODS
卷 9, 期 6, 页码 -出版社
MDPI
DOI: 10.3390/foods9060744
关键词
folic acid; lactoferrin; interactions; molecular modeling; dietary; functional
资金
- project Excellence, performance and competitiveness in the Research, Development and Innovation activities at Dunarea de Jos University of Galati, - Romanian Ministry of Research and Innovation [14PFE/17.10.2018]
The impact of thermal treatment on the ability of lactoferrin (FL) to bind folic acid (FA) was investigated by employing fluorescence spectroscopy, molecular dynamics and docking tests. The structural and conformational particularities of LF upon heating at 80 degrees C and 100 degrees C were first estimated based on the intrinsic fluorescence changes in respect to the native protein. The emission spectra indicated gradual unfolding events accompanied by Trp exposure with increasing temperature. In agreement with the experimental results, molecular modeling investigations showed that the secondary and tertiary structure of LF are slightly affected by the thermal treatment. Some minor unfolding events related particularly to the alpha-helical regions of LF were observed when the temperature increased to 100 degrees C. The LF fluorescence quenching upon FA addition indicated that a static mechanism stands behind LF-FA complex formation. Regardless of the simulated temperature, the hydrogen bonds played an important role in regulating the interaction between the protein and ligand. FA binding to LF equilibrated at different temperatures occurred spontaneously, and all complexes displayed good thermodynamic stability. The obtained results support the suitability of LF as biocompatible material, for obtaining micro- and nanoparticles for delivery of dietary supplements or for enhancing the functionality of target delivery systems.
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