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Small peptides inhibit gut trypsin-like proteases and impair Anticarsia gemmatalis (Lepidoptera: Noctuidae) survival and development.
Pest Manag Sci. 2021 Apr; 77(4):1714-1723.PM

Abstract

BACKGROUND

Anticarsia gemmatalis larvae are key defoliating pests of soybean plants. Inorganic insecticides, harmful to the environment and human health, are the main molecules used in the control of this pest. To apply more sustainable management methods, organic molecules with high specificities, such as proteinaceous protease inhibitors, have been sought. Thus, molecular docking studies, kinetics assays, and biological tests were performed to evaluate the inhibitory activity of two peptides (GORE1 and GORE2) rationally designed to inhibit trypsin-like enzymes, which are the main proteases of A. gemmatalis midgut.

RESULTS

The molecular docking simulations revealed critical hydrogen bonding patterns of the peptides with key active site residues of trypsin-like proteases of A. gemmatalis and other Lepidopteran insects. The negative values of binding energy indicate that hydrogen bonds potentiate the tight binding of the peptides with trypsin-like proteases, predicting an effective inhibition. The inhibition's rate constants (Ki) were 0.49 and 0.10 mM for GORE1 and GORE2, resulting in effective inhibition of the activity trypsin on the L-BApNA substrate in the in vitro tests, indicating that the peptide GORE2 has higher inhibitory capacity on the A. gemmatalis trypsins. In addition, the two peptides were determined to be reversible competitive inhibitors. The in vivo test demonstrated that the peptides harm the survival and development of A. gemmatalis larvae.

CONCLUSION

These results suggest that these peptides are potential candidates in the management of A. gemmatalis larvae and provide baseline information for the design of new trypsin-like inhibitors based on peptidomimetic tools. © 2020 Society of Chemical Industry.

Authors+Show Affiliations

Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Brazil. Instituto de Biotecnologia Aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Brazil.Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Brazil. Instituto de Biotecnologia Aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Brazil.Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Brazil. Instituto de Biotecnologia Aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Brazil. Center of Analysis of Biomolecules, NuBioMol, Universidade Federal de Viçosa, Viçosa, Brazil.Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Brazil. Instituto de Biotecnologia Aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Brazil.Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Brazil. Instituto de Biotecnologia Aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Brazil.Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Brazil. Instituto de Biotecnologia Aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Brazil.Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Brazil. Instituto de Biotecnologia Aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Brazil.Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Brazil. Instituto de Biotecnologia Aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Brazil. Center of Analysis of Biomolecules, NuBioMol, Universidade Federal de Viçosa, Viçosa, Brazil.Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Brazil. Instituto de Biotecnologia Aplicada à Agropecuária, BIOAGRO-UFV, Viçosa, Brazil.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

33200876

Citation

de Almeida Barros, Rafael, et al. "Small Peptides Inhibit Gut Trypsin-like Proteases and Impair Anticarsia Gemmatalis (Lepidoptera: Noctuidae) Survival and Development." Pest Management Science, vol. 77, no. 4, 2021, pp. 1714-1723.
de Almeida Barros R, Meriño-Cabrera Y, Vital CE, et al. Small peptides inhibit gut trypsin-like proteases and impair Anticarsia gemmatalis (Lepidoptera: Noctuidae) survival and development. Pest Manag Sci. 2021;77(4):1714-1723.
de Almeida Barros, R., Meriño-Cabrera, Y., Vital, C. E., da Silva Júnior, N. R., de Oliveira, C. N., Lessa Barbosa, S., Marques Gonçalves Assis, J. V., Ramos, H. J., & de Almeida Oliveira, M. G. (2021). Small peptides inhibit gut trypsin-like proteases and impair Anticarsia gemmatalis (Lepidoptera: Noctuidae) survival and development. Pest Management Science, 77(4), 1714-1723. https://doi.org/10.1002/ps.6191
de Almeida Barros R, et al. Small Peptides Inhibit Gut Trypsin-like Proteases and Impair Anticarsia Gemmatalis (Lepidoptera: Noctuidae) Survival and Development. Pest Manag Sci. 2021;77(4):1714-1723. PubMed PMID: 33200876.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Small peptides inhibit gut trypsin-like proteases and impair Anticarsia gemmatalis (Lepidoptera: Noctuidae) survival and development. AU - de Almeida Barros,Rafael, AU - Meriño-Cabrera,Yaremis, AU - Vital,Camilo E, AU - da Silva Júnior,Neilier R, AU - de Oliveira,Cauê N, AU - Lessa Barbosa,Samuel, AU - Marques Gonçalves Assis,João V, AU - Ramos,Humberto Jo, AU - de Almeida Oliveira,Maria G, Y1 - 2020/12/04/ PY - 2020/09/02/revised PY - 2020/01/27/received PY - 2020/11/17/accepted PY - 2020/11/18/pubmed PY - 2021/3/18/medline PY - 2020/11/17/entrez KW - binding energy KW - enzymes KW - inhibition KW - pharmacophoric profile SP - 1714 EP - 1723 JF - Pest management science JO - Pest Manag Sci VL - 77 IS - 4 N2 - BACKGROUND: Anticarsia gemmatalis larvae are key defoliating pests of soybean plants. Inorganic insecticides, harmful to the environment and human health, are the main molecules used in the control of this pest. To apply more sustainable management methods, organic molecules with high specificities, such as proteinaceous protease inhibitors, have been sought. Thus, molecular docking studies, kinetics assays, and biological tests were performed to evaluate the inhibitory activity of two peptides (GORE1 and GORE2) rationally designed to inhibit trypsin-like enzymes, which are the main proteases of A. gemmatalis midgut. RESULTS: The molecular docking simulations revealed critical hydrogen bonding patterns of the peptides with key active site residues of trypsin-like proteases of A. gemmatalis and other Lepidopteran insects. The negative values of binding energy indicate that hydrogen bonds potentiate the tight binding of the peptides with trypsin-like proteases, predicting an effective inhibition. The inhibition's rate constants (Ki) were 0.49 and 0.10 mM for GORE1 and GORE2, resulting in effective inhibition of the activity trypsin on the L-BApNA substrate in the in vitro tests, indicating that the peptide GORE2 has higher inhibitory capacity on the A. gemmatalis trypsins. In addition, the two peptides were determined to be reversible competitive inhibitors. The in vivo test demonstrated that the peptides harm the survival and development of A. gemmatalis larvae. CONCLUSION: These results suggest that these peptides are potential candidates in the management of A. gemmatalis larvae and provide baseline information for the design of new trypsin-like inhibitors based on peptidomimetic tools. © 2020 Society of Chemical Industry. SN - 1526-4998 UR - https://www.unboundmedicine.com/medline/citation/33200876/Small_peptides_inhibit_gut_trypsin_like_proteases_and_impair_Anticarsia_gemmatalis__Lepidoptera:_Noctuidae__survival_and_development_ DB - PRIME DP - Unbound Medicine ER -