Malaria remains a leading cause of global morbidity and mortality, and the World Health Organization estimates 282 million cases and 610,000 deaths in 2024 alone, against the emerging partial artemisinin resistance and persistent insecticide resistance. Antimicrobial peptide (AMPs) native to the mosquito innate immune system are increasingly being explored as scaffolds for next-generation antiplasmodial agents, because their membrane and structure-disruptive mechanisms are considered less prone to rapid resistance selection than conventional small-molecule antimalarials. This study used structure-based in silico docking to evaluate the interaction of an insect defensin peptide (Defensin A; PDB: 2E3E) with two Plasmodium falciparum antigens and one Plasmodium vivax antigen that together span distinct, biologically critical stages of the parasite life cycle: the transmission-blocking waxing antigen Pfs25 (PDB: 8EZK), sporozoite motility and hepatocyte-invasion protein TRAP containing Thrombospondin Type-1 Repeat (TSR) domain (PDB: 2BBX), and the apical membrane antigen 1 (AMA-1) structural template (PDB: 1W8K), selected as a representative AMA-1 orthologue because of the conserved PAN-fold architecture among Plasmodium species. Structures were retrieved from the RCSB Protein Data Bank and docked pairwise using the Frontier-transform-based HexServer platform. The resulting complexes were visualized and inspected for interfacial contacts in PyMol. Defense A engaged all three targets, but with markedly different predicted energetics: the Defensin A-AMA-1(-595.61) produced the most favorable predicted docking score among the tested targets than entire Defensin A-Pfs25 (-394.44) or Defensin A-TRAP (-393.25), and involved a broader predicted interface (Tyr33-Leu384 and Lys35-Val382) relative to the single contact pair identified for each of the other two complexes. These preliminary findings suggest that defensin-class peptides may preferentially engage AMA-1 and support prioritization of this interaction for downstream experimental (in vitro and in vivo) antiplasmodial validation.