Analysis of the Antibacterial Targets of Maackiain Based on Network Pharmacology and Molecular Docking

Abstract

Abstract

Background: Antimicrobial resistance is a growing global concern, with bacterial, fungal, and viral infections posing significant threats to public health. Traditional antibiotics have become less effective due to the emergence of resistant strains, leading to an urgent need for novel antimicrobial agents. Maackiain, a bioactive compound derived from natural sources, has shown potential antimicrobial properties. Understanding the mechanisms through which maackiain exerts its antibacterial effects could provide valuable insights for the advancement of new therapeutic strategies. The present study seeks to investigate the antibacterial targets and pathways of maackiain using network pharmacology to identify its potential as an effective antimicrobial agent.

Methods: Relevant databases were utilized to identify maackiain and antibacterial-related targets. Drug-disease target intersections were predicted, and a PPI network was constructed. GO enrichment assessment and KEGG pathway exploration were carried out.

Results: The sum total of 50 intersecting target genes between maackiain and antibacterial-related pathways were identified. Core targets included NFKB1, ESR1, MTOR, ACE, PARP1, and MAPK1. GO enrichment analysis uncovered remarkable procedures like inflammatory response, protein phosphorylation, and innate immune response. Cellular component analysis highlighted plasma membrane, cytosol, cytoplasm, and membrane-associated structures. Molecular function analysis identified binding of protein, binding of identical protein, binding of ATP, and binding of enzyme. KEGG pathway analysis demonstrated significant involvement in the HIF-1 signaling pathway, chemical carcinogenesis-receptor activation, AGE-RAGE signaling pathway in diabetic complications, and arginine and proline metabolism. Molecular docking results indicated that Maackiain exhibited binding energies below -6.9 kcal/mol with core targets.

Conclusion: The core antibacterial targets of maackiain include NFKB1, ESR1, MTOR, ACE, and PARP1. Further experimental validation is warranted.