Docking and Antimicrobial Potential of Lactoferrin in Capra hircus: An In-silico Approach

Abstract

Lactoferrin is an iron-binding glycoprotein with multiple functions, naturally occurring in milk, saliva, tears, and other mucosal secretions, and has been shown to possess antimicrobial and antiviral properties. This investigation aimed to examine the composition and role of lactoferrin in Capra hircus using computational techniques. In-silico tools were employed to characterize lactoferrin and explore its molecular interactions, including peptide cutter for enzymatic cleavage, CAMP for antimicrobial prediction, and molecular docking to assess its binding affinity with bacterial targets. Among the 54 peptides derived from lactoferrin, 13 positively charged peptides demonstrated significant antibacterial properties, validated through antimicrobial prediction tools. For structural validation, only the peptide with the highest length was selected for 3D modeling and analysis. The 3D structural model confirmed high similarity to known lactoferrin structures, highlighting conserved regions critical for antibacterial activity. The predicted structural model provided insights into the dynamic behavior of lactoferrin, exhibiting high similarity to other known lactoferrin structures which indicates its conserved nature across species in mammals. These findings highlight key regions involved in protein-protein interactions and structural characterization that reinforce its antimicrobial properties. Molecular docking and ADMET analysis manifest the best drug candidate that exhibit antimicrobial properties. Best docked compound enterobactin violate the toxicity profile. This study sets the stage for further experimental validation of these predicted interactions while shedding light on the molecular mechanisms underlying the multifunctional properties of lactoferrin in Capra hircus.