Noncompetitive tight-binding inhibition of Anticarsia gemmatalis trypsins by Adenanthera pavonina protease inhibitor affects larvae survival.

Autor: Meriño-Cabrera Y; Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Minas Gerais, Brazil.; Instituto de Biotecnologia Aplicada à Agropecuaria, BIOAGRO-UFV, Viçosa, Minas Gerais, Brazil., de Oliveira Mendes TA; Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Minas Gerais, Brazil.; Instituto de Biotecnologia Aplicada à Agropecuaria, BIOAGRO-UFV, Viçosa, Minas Gerais, Brazil., Castro JGS; Instituto de Biotecnologia Aplicada à Agropecuaria, BIOAGRO-UFV, Viçosa, Minas Gerais, Brazil.; Departamento de Ciencias Exatas, Universidade Estadual de Londrina, Londrina, Paraná, Brazil., Barbosa SL; Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Minas Gerais, Brazil.; Instituto de Biotecnologia Aplicada à Agropecuaria, BIOAGRO-UFV, Viçosa, Minas Gerais, Brazil., Macedo MLR; Laboratório de Purificação de Proteínas e suas Funções Biológicas, Unidade de Tecnologia de Alimentos e da Saúde Pública, Universidade Federal de Mato Grosso do Sul, Campo Grande, Mato Grosso do Sul, Brazil., de Almeida Oliveira MG; Departamento de Bioquímica e Biologia Molecular, Universidade Federal de Viçosa, Viçosa, Minas Gerais, Brazil.; Instituto de Biotecnologia Aplicada à Agropecuaria, BIOAGRO-UFV, Viçosa, Minas Gerais, Brazil.
Jazyk: angličtina
Zdroj: Archives of insect biochemistry and physiology [Arch Insect Biochem Physiol] 2020 Jul; Vol. 104 (3), pp. e21687. Date of Electronic Publication: 2020 Apr 27.
DOI: 10.1002/arch.21687
Abstrakt: The economic loss in soybean crops caused by the Lepidoptera insects has encouraged the search for new strategies to control this pest, which are currently based on synthetic insecticides. This paper evaluated the ability of ApTI (Adenanthera pavonina trypsin inhibitor) to inhibit trypsin-like proteins from Anticarsia gemmatalis by docking, molecular dynamics, and enzymatic and survival assay. The docking and molecular dynamic simulation between trypsin and ApTI were performed using the program CLUSPRO and NAMD, respectively. The inhibitory constant K i and the inhibition type were determined through chromogenic assays. The survival assay of neonatal larvae under treatment with artificial diet supplemented with ApTI was also performed. The ApTI binding site was predicted to block substrate access to trypsin due to four interactions with the enzyme, producing a complex with a surface area of 1,183.7 Å 2 . The kinetic analysis revealed a noncompetitive tight-binding mechanism. The survival curves obtained using Kaplan-Meier estimators indicated that the highest larvae mortality was 60%, using 1.2 mg of ApTI per 100 ml of artificial diet. The in vitro, in vivo, and in silico studies demonstrated that ApTI is a strong noncompetitive inhibitor of trypsin with biotechnological potential for the control of A. gemmatalis insect.
(© 2020 Wiley Periodicals, Inc.)
Databáze: MEDLINE
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