Moreno-Cordova Elena N, Alvarez-Armenta Andres, Garcia-Orozco Karina D, Arvizu-Flores Aldo A, Islas-Osuna Maria A, Robles-Zepeda Ramon E, Lopez-Zavala Alonso A, Laino Aldana, Sotelo-Mundo Rogerio R
Laboratorio de Estructura Biomolecular, Centro de Investigación en Alimentación y Desarrollo, A. C., Hermosillo, Sonora, Mexico.
Departamento de Microbiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Cuernavaca, Morelos, 62210, Mexico.
Heliyon. 2024 Jul 3;10(13):e34036. doi: 10.1016/j.heliyon.2024.e34036. eCollection 2024 Jul 15.
spp. spiders can cause serious public health issues. Chemical control is commonly used, leading to health and environmental problems. Identifying molecular targets and using them with natural compounds can help develop safer and eco-friendlier biopesticides. We studied the kinetics and predicted structural characteristics of arginine kinase (EC 2.7.3.3) from (AK), a key enzyme in the energy metabolism of these organisms. Additionally, we explored (-)-epigallocatechin gallate (EGCG), a green tea flavonoid, as a potential lead compound for the AK active site through fluorescence and analysis, such as molecular docking and molecular dynamics (MD) simulation and MM/PBSA analyses. The results indicate that AK is a highly efficient enzyme ( 0.14 mM, 0.98 mM, 93 s, / 630 s mM, / 94 s mM), which correlates with its structure similarity to others AKs (such as , , and ) and might be related to its important function in the spider's energetic metabolism. Furthermore, the MD and MM/PBSA analysis suggests that EGCG interacted with AK, specifically at ATP/ADP binding site (RMSD <1 nm) and its interaction is energetically favored for its binding stability (-40 to -15 kcal/mol). Moreover, these results are supported by fluorescence quenching analysis ( 58.3 μM and 1.71 × 10 M). In this context, AK is a promising target for the chemical control of , and EGCG could be used in combination with conventional pesticides to manage the population of species in urban areas.
蜘蛛物种会引发严重的公共卫生问题。化学防治方法被广泛使用，但会导致健康和环境问题。识别分子靶点并将其与天然化合物结合使用，有助于开发更安全、更环保的生物农药。我们研究了来自[蜘蛛名称]的精氨酸激酶（EC 2.7.3.3）（AK）的动力学和预测结构特征，AK是这些生物能量代谢中的关键酶。此外，我们通过荧光以及诸如分子对接、分子动力学（MD）模拟和MM/PBSA分析等方法，探索了绿茶类黄酮（-）-表没食子儿茶素没食子酸酯（EGCG）作为AK活性位点的潜在先导化合物。结果表明，AK是一种高效酶（Km 0.14 mM，Vmax 0.98 mM，kcat 93 s⁻¹，kcat/Km 630 s⁻¹ mM⁻¹，kcat/Ki 94 s⁻¹ mM⁻¹），这与其与其他AKs（如[列举的其他AKs名称]）的结构相似性相关，并且可能与其在蜘蛛能量代谢中的重要功能有关。此外，MD和MM/PBSA分析表明，EGCG与AK相互作用，特别是在ATP/ADP结合位点（RMSD <1 nm），并且其相互作用因其结合稳定性在能量上是有利的（-40至-15 kcal/mol）。此外，这些结果得到了荧光猝灭分析的支持（Ksv 58.3 μM和Kq 1.71×10¹² M⁻¹ s⁻¹）。在此背景下，AK是蜘蛛化学防治的一个有前景的靶点，并且EGCG可与传统农药联合使用，以控制城市地区蜘蛛物种的数量。
