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<p>Many plants are known to contain proteinase inhibitors in their vegetative parts and seeds, which play important role as defence molecules to overcome biotic and abiotic stresses. <i>Cocculus hirsutus</i> trypsin inhibitor (ChTI), isolated from leaves of <i>Cocculus hirsutus</i> is characterized to be stable protein at temperature 70&#xa0;°C and pH 7–9. In vitro experiments show that ChTI inhibits trypsin and exhibits deleterious effect on growth and development of lepidopteron insects that have trypsin like gut proteinase activity. However, these insects successfully adapt to proteinase inhibitors of their host plants by switching the expression of proteinase genes. Thus, it is interesting to study the interaction between proteinase inhibitors from non-host plant and gut proteinases. In silico interaction of trypsin was carried out using the predicted three dimensional structure of ChTI. Docking studies suggest that ChTI is a non canonical type of inhibitor and form stable inhibitor complexes with Trypsin and Chymotrypsin.</p>

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Structural elucidation of Cocculus hirsutus trypsin inhibitor and insights into its mechanism of action

  • 期刊论文

  • 发表日期：

    2025年5月7日

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  • Manushree Venkataswamy Reddy,
  • Varadhahalli Devaraj,
  • Prashantha Karunakar,
  • Vivek Chandramohan,
  • Doddananjappa Theertha Prasad

摘要

Many plants are known to contain proteinase inhibitors in their vegetative parts and seeds, which play important role as defence molecules to overcome biotic and abiotic stresses. Cocculus hirsutus trypsin inhibitor (ChTI), isolated from leaves of Cocculus hirsutus is characterized to be stable protein at temperature 70 °C and pH 7–9. In vitro experiments show that ChTI inhibits trypsin and exhibits deleterious effect on growth and development of lepidopteron insects that have trypsin like gut proteinase activity. However, these insects successfully adapt to proteinase inhibitors of their host plants by switching the expression of proteinase genes. Thus, it is interesting to study the interaction between proteinase inhibitors from non-host plant and gut proteinases. In silico interaction of trypsin was carried out using the predicted three dimensional structure of ChTI. Docking studies suggest that ChTI is a non canonical type of inhibitor and form stable inhibitor complexes with Trypsin and Chymotrypsin.