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Noncompetitive tight-binding inhibition of Anticarsia gemmatalis trypsins by Adenanthera pavonina protease inhibitor affects larvae survival.
Archives of Insect Biochemistry and Physiology ( IF 2.2 ) Pub Date : 2020-04-27 , DOI: 10.1002/arch.21687
Yaremis Meriño-Cabrera 1, 2 , Tiago A de Oliveira Mendes 1, 2 , José G S Castro 2, 3 , Samuel L Barbosa 1, 2 , Maria L R Macedo 4 , Maria G de Almeida Oliveira 1, 2
Affiliation  

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 Ki 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 Å2. 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.

中文翻译:

Adenanthera pavonina蛋白酶抑制剂对竞争性双生抗胰蛋白酶的非竞争性紧密结合抑制作用会影响幼虫的存活。

鳞翅目昆虫造成的大豆作物的经济损失鼓励寻找控制这种害虫的新策略,目前该策略以合成杀虫剂为基础。本文通过对接,分子动力学以及酶促和存活分析评估了ApTI(Adenanthera pavonina胰蛋白酶抑制剂)抑制来自双生抗龋的胰蛋白酶样蛋白的能力。分别使用CLUSPRO和NAMD程序在胰蛋白酶和ApTI之间进行对接和分子动力学模拟。抑制常数K i通过显色法测定其抑制类型。还进行了人工增补ApTI饮食治疗的新生幼虫的存活率测定。所述APTI结合位点预测到框基板访问与酶胰蛋白酶由于4间的相互作用,产生一个复用的1,183.7埃的表面积2。动力学分析揭示了一种非竞争性的紧密结合机制。使用Kaplan-Meier估算器获得的存活曲线表明,每100毫升人工饮食使用1.2毫克ApTI可以得出最高的幼虫死亡率为60%。体外,体内和计算机研究表明,ApTI是胰蛋白酶的一种强大的非竞争性抑制剂,具有控制双歧杆菌昆虫的生物技术潜力。
更新日期:2020-04-27
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