Fluorometric study on the interaction between lomefloxacin and bovine lactoferrin

Area of Science:

• Biochemistry
• Biophysics
• Pharmacology

Background:

• Bovine lactoferrin (BLf) is a key protein with antimicrobial properties.
• Understanding drug interactions with BLf is crucial for drug delivery and efficacy.
• Lomefloxacin is a fluoroquinolone antibiotic with potential interactions in biological systems.

Purpose of the Study:

• To investigate the binding mechanism between lomefloxacin and bovine lactoferrin (BLf).
• To quantify the binding parameters, including binding constant (K) and number of binding sites (n).
• To explore the impact of lomefloxacin on the conformational changes of BLf.

Main Methods:

• Fluorescence spectroscopy was employed to study the binding interaction.
• Fluorescence quenching method was used to determine binding constants and sites.
• Foörster's theory of energy transfer was applied to calculate binding distance and efficiency.
• Synchronous fluorescence spectroscopy analyzed conformational alterations.

Main Results:

• A strong binding interaction between lomefloxacin and BLf was observed.
• Binding parameters (K and n) were successfully determined.
• Energy transfer parameters (r and E) indicated a specific binding mechanism.
• Lomefloxacin was found to induce noticeable changes in BLf conformation.

Conclusions:

• Lomefloxacin exhibits a strong affinity for bovine lactoferrin.
• The interaction involves energy transfer and specific binding sites.
• Lomefloxacin binding induces conformational changes in BLf, potentially affecting its function.