In silico characterization, physiochemical analysis, and antifungal evaluation of the Zea mays PR-1 protein.

Pathogenesis-related protein 1 (PR-1) is a critical component of plant defense mechanisms, exhibiting significant antifungal activity. This study focused on the PR-1 protein from Zea mays and five other plant species (Triticum aestivum, Hordeum vulgare, Oryza sativa, Avena sativa, and Secale cereale) to explore their physicochemical, structural, and functional characteristics. The PR-1 gene from Z. mays was isolated and expressed in Escherichia coli BL21-DE3 cells, enabling structural characterization. Recombinant expression in E. coli enabled structural characterization and functional studies of the PR-1 protein, laying a foundation for future experiments. Sequence analysis revealed high similarity (65-90%) among PR-1 proteins across species, although physicochemical properties varied based on plant origin. Structural analysis showed a conserved beta-barrel structure surrounded by alpha-helices in all PR-1 proteins. In addition to in silico and structural characterization, antifungal bioassays were performed using the purified recombinant PR-1 protein against Fusarium oxysporum, a major fungal phytopathogen. These assays demonstrated notable antifungal activity, supporting the predicted defense role of PR-1 and laying experimental groundwork for its potential use in developing fungi-resistant transgenic crops.