Crystal structure of Kunitz-type trypsin inhibitor: Entomotoxic effect of native and encapsulated protein targeting gut trypsin of Tribolium castaneum Herbst.

Autor:	Mehmood S; Institute of Botany, Bahauddin Zakariya University, Multan 60800, Pakistan., Thirup SS; Department of Molecular Biology and Genetics, Centre for Structural Biology, Aarhus University, Aarhus 8000, Denmark., Ahmed S; Department of Entomology, Bahauddin Zakariya University, Multan 60800 Pakistan., Bashir N; Institute of Chemical Sciences, Bahauddin Zakariya University, Multan 60800 Pakistan., Saeed A; Institute of Botany, Bahauddin Zakariya University, Multan 60800, Pakistan., Rafiq M; Institute of Botany, Bahauddin Zakariya University, Multan 60800, Pakistan., Saeed Q; Department of Entomology, Bahauddin Zakariya University, Multan 60800 Pakistan., Najam-Ul-Haq M; Institute of Chemical Sciences, Bahauddin Zakariya University, Multan 60800 Pakistan., Khaliq B; Botany Department, University of Okara, Okara 56300, Pakistan., Ibrahim M; Department of Biosciences, COMSATS University Islamabad (Sahiwal Campus), Sahiwal 57000, Pakistan., Alonazi WB; Health Administration Department, College of Business Administration, King Saud University, P. O. Box 800, Riyadh 11421, Saudi Arabia., Akrem A; Institute of Botany, Bahauddin Zakariya University, Multan 60800, Pakistan.
Jazyk:	angličtina
Zdroj:	Computational and structural biotechnology journal [Comput Struct Biotechnol J] 2024 Aug 03; Vol. 23, pp. 3132-3142. Date of Electronic Publication: 2024 Aug 03 (Print Publication: 2024).
DOI:	10.1016/j.csbj.2024.07.023
Abstrakt:	Trypsin inhibitors are known to act against insect pests by inhibiting proteases of the digestive tract. In this study, we report structural and functional characterization of ∼ 19 kDa Albizia procera Kunitz-type trypsin inhibitor (ApKTI) protein with potential bio-insecticidal applications. Crystal structure of ApKTI protein has been refined to 1.42 Å and molecular structure (8HNR) showed highly beta sheeted conformation including 12 beta sheets, 15 loops and two small alpha helices. Docking between predicted model of Tribolium castaneum trypsin (TcPT) and 8HNR produced a stable complex (-11.3 kcal/mol) which reflects the inhibitory potential of ApKTI against insect gut trypsin. Significant mortality was observed in all life stages of T. castaneum including egg, larvae, pupae and adults with a 3.0 mg native ApKTI treatment in comparison to negative control. Although standard trypsin inhibitor ( Glycine max trypsin inhibitors; GmKTI; 3.0 mg) produced maximum reduction against all above life stages; however, a non-significant mortality difference was observed in comparison to 3.0 mg native ApKTI. The study further explores the synthesis and characterization of Graphene (GNPs) and Zinc oxide (ZnONPs) nanoparticles, followed by the optimization of ApKTI and GmKTI loading on both nanoparticles to evaluate their enhanced insecticidal effectiveness. Encapsulated proteins showed significant mortality against T. castaneum across all concentrations, with GNPs proving more effective than ZnONPs. Additionally, encapsulated GmKTI produced significant mortality of eggs compared to loaded ApKTI treatments while other life stages were non-significantly affected by two proteins. This research highlights the importance of encapsulated ApKTI protein for eco-friendly pest management strategies. Competing Interests: The authors declare the following financial interests/personal relationships which may be considered as potential competing interests, Dr. Ahmed Akrem reports a relationship with Bahauddin Zakariya University that includes: employment. If there are other authors, they declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (© 2024 The Authors.)
Databáze:	MEDLINE
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