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Merrill) productivity is severely impacted by the velvetbean caterpillar\n                    <jats:italic>Anticarsia gemmatalis<\/jats:italic>\n                    H\u00fcbner, 1818 (Lepidoptera: Erebidae), a major defoliating pest in soybean\u2010producing regions. Current management strategies rely heavily on chemical insecticides, which are associated with environmental risks and the development of resistance. Protease inhibitors have emerged as a promising alternative, as protein digestion in lepidopteran larvae is primarily mediated by trypsin\u2010like serine proteases. In this context, the rational design of short inhibitory peptides represents a potential strategy for developing selective and environmentally safer pest control agents. This study introduces the regulatory pro\u2010region of trypsinogen as a previously underexplored scaffold for the rational design of competitive peptide inhibitors targeting digestive trypsin\u2010like enzymes in agricultural insect pests. Fifteen peptides derived from the trypsinogen pro\u2010region were initially\n                    <jats:italic>screened in silico<\/jats:italic>\n                    against\n                    <jats:italic>A. gemmatalis<\/jats:italic>\n                    trypsin\u2010like enzymes. Molecular docking analyses revealed favorable binding energies and interactions with residues located in the catalytic region. Among the candidates, the peptide Pep12 (designated GORE3) was selected for further optimization by substituting amino acids at the P1 position, yielding the analogs GORE4 and GORE5. Enzyme inhibition assays with bovine trypsin and partially purified\n                    <jats:italic>A. gemmatalis<\/jats:italic>\n                    trypsin\u2010like enzymes demonstrated that all peptides are competitive inhibitors. The inhibition constants (Ki) obtained for\n                    <jats:italic>A. gemmatalis<\/jats:italic>\n                    enzymes were 1.80\u2009mM for GORE3, 1.63\u2009mM for GORE4, and 0.78\u2009mM for GORE5, with GORE5 exhibiting the lowest Ki among the evaluated peptides, although its inhibitory affinity remained within the millimolar range. Collectively, these findings underscore the potential of trypsinogen\u2010derived peptides as promising scaffolds for developing peptide\u2010based inhibitors targeting insect digestive proteases.\n                  <\/jats:p>","DOI":"10.1002\/arch.70224","type":"journal-article","created":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T18:26:46Z","timestamp":1791138406000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Trypsinogen Pro\u2010Region as a Molecular Scaffold for the Design of Competitive Peptide Inhibitors of Trypsin\u2010Like Proteases"],"prefix":"10.1002","volume":"123","author":[{"given":"Geisiane Aparecida","family":"Mariano","sequence":"first","affiliation":[{"name":"Laboratory of Enzymology and Biochemistry of Proteins and Peptides, Department of Biochemistry and Molecular Biology Universidade Federal de Vi\u00e7osa, UFV, BIOAGRO\/INCT\u2010IPP Vi\u00e7osa Minas Gerais 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