Abstract
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.
Highlights
Tetracycline hydrochloride (TCH, as shown at Figure 1A), an important class of tetracycline antibiotics, has become a widely used veterinary medicine for therapeutic and prophylactic purposes [1]
The results obtained from experiments showed that tetracycline hydrochloride (TCH) interacted with Bovine lactoferrin (bLf) and caused a change of bLf structure
circular dichroism spectra (CD) spectra further analyzed the transformation of the secondary component in the process of structural change and confirmed that the addition of TCH caused the protein structure to become loose
Summary
Tetracycline hydrochloride (TCH, as shown at Figure 1A), an important class of tetracycline antibiotics, has become a widely used veterinary medicine for therapeutic and prophylactic purposes [1]. As a very popular nutrient, milk consumption is increasing year by year with the improvement of people’s living standards [4]. It can provide people with rich protein, it is not clear whether the remaining antibiotics in milk have affected the structure and function of milk proteins, and whether the effects will cause harm to humans. It is important to study the effect of antibiotics residues in milk on bovine proteins
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