Peptidic product derived from trypsin autolysis modulates insect digestive proteases and supports plant biochemical defense

Docking and bioassays collectively demonstrate that GORE 3 interacts with trypsin-like proteases through a robust, multisite binding mode, resulting in competitive inhibition and measurable physiological effects in S. frugiperda. Although less potent than benzamidine based on K_i values, GORE3's isoform-spanning interactions and its influence on digestive and developmental parameters highlight the relevance of studying protease-inhibitor peptides as biochemical models for understanding lepidopteran digestive physiology. Future work should investigate peptide stability, compensatory digestive responses, and performance under diverse biological conditions to better clarify the biological significance of these interactions. © 2026 The Author(s). Pest Management Science published by John Wiley & Sons Ltd on behalf of Society of Chemical Industry.