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Crystal Structure of Kunitz-Type Trypsin Inhibitor: Entomotoxic Effect of Native and Encapsulated Protein Targeting Gut Protease of Trogoderma Granarium Everts
Author(s)
Sohaib Mehmood Institute of Botany, Bahauddin Zakariya University, Multan, Pakistan
Soren SkouThirup Department of Molecular Biology and Genetics, Center for Structural Biology, Aarhus University, Aarhus, Denmark
Ahsan Saeed Institute of Botany, Bahauddin Zakariya University, Multan, Pakistan
Sarah Ahmed Department of Entomology, Bahauddin Zakariya University, Multan, Pakistan
Maria Rafiq Institute of Botany, Bahauddin Zakariya University, Multan, Pakistan
Qamar Saeed Department of Entomology, Bahauddin Zakariya University, Multan, Pakistan
M. Najam-ul-Haq Department of Biochemistry, Institute of Chemical Sciences, Bahauddin Zakariya University, Multan, Pakistan
Binish Khaliq Botany Department, University of Okara, Okara, Pakistan
Ahmed Akrem Institute of Botany, Bahauddin Zakariya University, Multan, Pakistan
Abstract
Trypsin inhibitors are commonly known to act against insect pests by inhibiting proteases of the digestive tract, interfering in pest development and proliferation. Albizia procera Kunitz-type trypsin inhibitor (ApKTI) protein was purified by AKTA purifier and identification was done via LC-MS/MS. Purified protein (5 mg/ml) was put for 192 petential crystallization conditions manually in sitting drop method by using commercially available kits comprising of different PEG recipes (Hampton Research). Needle shaped crystals (1.0 × 0.03 × 0.03 mm) appeared (0.1 M MES monohydrate; pH: 6.0, 25% PEG 400) after one week at 20°C. Remote X-ray diffraction data was collected at beamline P13 (100K) operated by EMBL Hamburg at the PETRA III storage ring (DESY, Hamburg, Germany). Images were obtained and data was processed by using XDS and refined to a crystallographic R-work 0.1625% and Rfree 0.183% with diffraction resolution of 1.4 A through PHENIX. Molecular structure showed highly beta sheeted conformation including 12 beta sheets, 15 loops and two small alpha helices. Stable ApKTI (PDB ID: 8HNR) and bovine trypsin (PDB ID: 1AQ7) docked complex showed binding energy of -14.7 kcal/mol (PRODIGY) and 255.08 kj/mol (PIMA) along salt-bridges, hydrogen bindings and non-bonded interactions. Insecticidal potential of ApKTI(1.0, 2.0 and 3.0 mg) was checked against Trogoderma granarium, a storage grains insect pest. Significant mortality of T. granarium adults was observed at highest dose (3.0 mg) in F1 generation while all protein doses reduced all life stages in F2 generation as compared to control. Next, ApKTI was encapsulated with graphene quantum dots (GQDs) and Zinc oxide quantum dots (ZnOQDs) to form a shell to protect biomolecule and prevent it from leaching out before reaching the targeted site. Encapsulated protein showed significant mortality against T. granarium at all concentrations as compared to native protein. Additionally, GQDs doses found more effective as compared to ZnOQDs against all life stages of T. granarium insect pest. Exploration of such potent molecules is the prerequisite of our time regarding the anticipation of post antibiotic era and the development of insect resistance against chemical pesticides.
Publication Details
Page(s) 45-45
DOI DOI not available
Published Journal: Abstract Book on Second International Conference on Recent Approaches in Plant Sciences (RAPS-23) 4-5 May 2023 , Volume: 0, Issue: 0, Year: 2023
Keywords
Crystal structure Albizia procera zinc oxide quantum dotes Kunitztype trypsin inhibitor ApKTI graphene quantum dots
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