Structural Characterization of the Staphylococcus aureus Targeting Lectin Peptides from Garlic (Allium sativum L) by Liquid Nitrogen Grinding Coupled with the Proteomic and Antimicrobial Mechanism Analysis.

Garlic has long been used as an antimicrobial spice and herbal remedy. The aim of this study was to isolate the antimicrobial agent in garlic water extract against Staphylococcus aureus (S. aureus) and investigate its antimicrobial mechanism. By an activity-guided separation, garlic lectin-derived peptides (GLDPs) with main molecular weight of around 12 kDa were extracted by liquid nitrogen grinding and identified with high bactericidal activity toward S. aureus, and the MIC was determined as 24.38 μg/mL. In-gel digestion-based proteomic analysis indicated that the peptide sequences were highly identical to the B strain of garlic protein lectin II. Structure analysis suggested that the secondary structure was strongly affected by lyophilization and thus resulted in the inactivation of GLDPs (P < 0.05). Mechanism study revealed that treatment of GLDPs resulted in cell membrane depolarization in a dose-dependent manner, and the disruptions of the cell wall and membrane integrities were observed under electric microscopies. GLDPs could successfully dock with cell wall component lipoteichoic acid (LTA) via van der Waals and conventional bonds in molecular docking analysis. These results suggested that GLDPs were responsible for the S. aureus targeting activity and might be promising candidates for antibiotic development against bacterial infection.