Abstract:Background: The complete understanding of feeding and reproduction strategies during metamorphosis of silkworm Bombyx mori is very essential, for that a comparative proteomics analysis was used to investigate the proteins extracted from the head of the larva and adult of Bombyx mori. Materials and Methods: Proteins were separated and identified by using 2D-PAGE and MALDI-TOF-TOF-MS analysis respectively. The functions of each proteins were annotated using STRAP GO analysis. The expression level of each protein… Show more
“…Thus, was identified a serpin inhibitor with a molecular mass of 38 ± 2 kDa. This mass coincides with other inhibitors serpin-like, Despite the variations in size, the inhibitors of this family have an approximate molecular mass of 40-50 kDa (Arunprasanna et al, 2017;Christen et al, 2012;Ragan et al, 2010;Toubarro et al, 2013;Xu et al, 2015).…”
New approaches are needed to reduce risks to the environment and natural enemies and to avoid or delay the onset of insecticide resistance. The use of insecticides based on proteinase inhibitors of hemolymph is an alternative for the control of Lepidoptera pests primarily by having low toxicity and short persistence in the environment. Thus, in this study, we describe the purification process and identification of protease inhibitors from hemolymph Anticarsia gemmatalis and their activities against trypsin enzymes. Furthermore, the three-dimensional (3D) structure of the inhibitor and binding mode to trypsin enzymes was determined, and the stability of the inhibitory activity in several pHs and temperature values was evaluated. The inhibitor was characterized as a serpin family inhibitor and named A. gemmatalis hemolymph serpin inhibitor (AHSI), with an approximate mass of 38 ± 2 kDa, highly stable to temperature and pH variations, and with inhibitory capacity on bovine trypsin and gut trypsin of A. gemmatalis demonstrated by calculated K i values and affinity energy through molecular docking, being a reversible competitive inhibitor that binds to the active site of
“…Thus, was identified a serpin inhibitor with a molecular mass of 38 ± 2 kDa. This mass coincides with other inhibitors serpin-like, Despite the variations in size, the inhibitors of this family have an approximate molecular mass of 40-50 kDa (Arunprasanna et al, 2017;Christen et al, 2012;Ragan et al, 2010;Toubarro et al, 2013;Xu et al, 2015).…”
New approaches are needed to reduce risks to the environment and natural enemies and to avoid or delay the onset of insecticide resistance. The use of insecticides based on proteinase inhibitors of hemolymph is an alternative for the control of Lepidoptera pests primarily by having low toxicity and short persistence in the environment. Thus, in this study, we describe the purification process and identification of protease inhibitors from hemolymph Anticarsia gemmatalis and their activities against trypsin enzymes. Furthermore, the three-dimensional (3D) structure of the inhibitor and binding mode to trypsin enzymes was determined, and the stability of the inhibitory activity in several pHs and temperature values was evaluated. The inhibitor was characterized as a serpin family inhibitor and named A. gemmatalis hemolymph serpin inhibitor (AHSI), with an approximate mass of 38 ± 2 kDa, highly stable to temperature and pH variations, and with inhibitory capacity on bovine trypsin and gut trypsin of A. gemmatalis demonstrated by calculated K i values and affinity energy through molecular docking, being a reversible competitive inhibitor that binds to the active site of
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