Journal
MOLECULES
Volume 23, Issue 8, Pages -Publisher
MDPI
DOI: 10.3390/molecules23081900
Keywords
bovine lactoferrin; tetracycline hydrochloride; mutil-spectral technique; microscale thermophoresis; molecular docking
Funding
- Program for Natural Science Foundation of Shandong province [ZR2016CM47]
Ask authors/readers for more resources
In this paper, the interaction between bovine lactoferrin (bLf) and tetracycline hydrochloride (TCH) was researched by microscale thermophoresis (MST), multi-spectroscopic methods, and molecular docking techniques. Normal fluorescence results showed that TCH effectively quenched the intrinsic fluorescence of bLf via static quenching. Moreover, MST confirmed that the combination force between bLf and TCH was very strong. Thermodynamic parameters and molecular docking further revealed that electrostatic forces, van der Waals, and hydrogen bonding forces played vital roles in the interaction between bLf and TCH. The binding distance and energy transfer efficiency between TCH and bLf were 2.81 nm and 0.053, respectively. Moreover, the results of circular dichroism spectra (CD), ultraviolet visible (UV-vis) absorption spectra, fluorescence Excitation-Emission Matrix (EEM) spectra, and molecular docking verified bLf indeed combined with TCH, and caused the changes of conformation of bLf. The influence of TCH on the functional changes of the protein was studied through the analysis of the change of the bLf surface hydrophobicity and research of the binding forces between bLf and iron ion. These results indicated that change in the structure and function of bLf were due to the interaction between bLf and TCH.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available