Characterization of the Interactions between Minocycline Hydrochloride and Trypsin with Spectroscopic and Molecular Docking Technology

In the current study, the interaction of minocycline hydrochloride (MC) and trypsin (TRP) was studied using fluorescence spectroscopy, synchronous fluorescence spectroscopy, three-dimensional fluorescence spectroscopy, UV-Vis spectroscopy, and molecular docking simulation techniques. The results show that the fluorescence quenching of trypsin at different degrees can be caused by minocycline hydrochloride at different temperatures. According to the Stern-Volmer equation, the fluorescence quenching type was static quenching. By calculating critical distance, we concluded that there is a possibility of non-radiative energy transfer between minocycline hydrochloride and trypsin. The effect of minocycline hydrochloride on the secondary structure of trypsin was demonstrated using ultraviolet spectroscopy. Synchronous fluorescence spectroscopy showed that minocycline hydrochloride could bind to tryptophan residues in trypsin, resulting in corresponding changes in the secondary structure of trypsin. Three-dimensional fluorescence spectroscopy showed that minocycline hydrochloride had a particular effect on the microenvironment of trypsin that led to changes in the secondary structure of trypsin. The molecular docking technique demonstrated that the binding of minocycline hydrochloride and trypsin was stable. Circular dichroism showed that the secondary structure of trypsin could be changed by minocycline hydrochloride.

 

Comments：

The current study investigated the interaction between minocycline hydrochloride (MC) and trypsin (TRP) using various spectroscopic and molecular docking techniques. The results indicated that MC can cause fluorescence quenching of TRP at different degrees, suggesting static quenching. The critical distance calculation suggested the possibility of non-radiative energy transfer between MC and TRP. The UV-Vis spectroscopy demonstrated that MC affects the secondary structure of TRP. Synchronous fluorescence spectroscopy indicated that MC can bind to tryptophan residues in TRP, resulting in changes in the secondary structure of TRP. Three-dimensional fluorescence spectroscopy revealed that MC has a specific effect on the microenvironment of TRP, leading to changes in its secondary structure. The molecular docking technique showed stable binding of MC and TRP. Circular dichroism suggested that MC can change the secondary structure of TRP.

Overall, this study provides a comprehensive understanding of the interaction between MC and TRP, highlighting its impact on the secondary structure of TRP. These findings can be valuable for future research in developing effective treatments for various diseases.

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