Study on the interactions between ginsenosides and lysozyme under acidic condition by ESI-MS and molecular docking

Area of Science:

• Biochemistry
• Pharmacology
• Molecular interactions

Background:

• Ginsenosides are key compounds in traditional medicine.
• Lysozyme is a crucial enzyme in the immune system.
• Understanding ginsenoside-protein interactions is vital for drug development.

Purpose of the Study:

• To investigate the noncovalent interactions between ginsenosides (Rg1, Re) and lysozyme.
• To compare the binding affinities and stabilities of different ginsenoside-lysozyme complexes.
• To elucidate the influence of pH on these molecular interactions.

Main Methods:

• Electrospray ionization mass spectrometry (ESI-MS) for complex detection and quantification.
• Molecular docking simulations to predict binding sites and interactions.
• Calculation of dissociation constants from mass spectra peak intensities.

Main Results:

• 1:1 and 2:1 noncovalent complexes of ginsenosides and lysozyme were identified.
• Ginsenoside Rg1 formed a more stable 1:1 complex with lysozyme than ginsenoside Re.
• Complex stability decreased with increasing acidity, with notable differences in 2:1 complex behavior.

Conclusions:

• Ginsenosides Rg1 and Re bind to the active sites of lysozyme.
• Acidity-induced conformational changes in lysozyme affect complex stability.
• Findings provide a basis for understanding ginsenoside efficacy and developing related therapeutics.