相关实验视频

Updated: Feb 19, 2026

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Published on: May 9, 2025

针对Leptospira interrogans中的GroEL自然抑制剂的计算识别:一个整合性的虚拟查和分子动态方法

Guneswar Sethi¹, Sthitaprajna Sahoo², Su-Cheol Han¹

¹Center for Large Animals Convergence Research, Korea Institute of Toxicology, Jeongeup-si, Jeollabuk-do, Republic of Korea.

Frontiers in cellular and infection microbiology

|February 18, 2026

概括

研究人员确定了针对GroEL的天然化合物,GroEL是莱普托斯匹拉生物膜形成的关键蛋白质. 这些化合物显示出作为新型治疗方法的承诺,用于治疗严重的动物传播疾病 - - 螺杆菌病.

科学领域:

微生物学微生物学
药物发现药物发现药物发现
计算化学计算化学

背景情况:

牛螺旋菌病是一种由Leptospira interrogans引起的动物传染病,它对公众健康和兽医造成了重大挑战.
病原体的持久性与生物膜形成有关,但缺乏有效的治疗方法.
GroEL chaperonin与生物膜形成和免疫性有关,使其成为潜在的治疗点.

研究的目的:

为了调查GroEL作为一个可行的药物点为Leptospira问询.
为了确定可能抑制GroEL活动的天然化合物.

主要方法:

543,503个自然化合物的基于结构的虚拟选.
分子对接,物理化学和药物动力学性质分析.
密度函数理论计算,分子动力学模拟和MM-PBSA结合的自由能量计算.

主要成果:

五种化合物 (F3385-2019,F1243-0200,F3139-0927,F2801-0179,F1864-0208) 显示出与GroEL (-10.34至 -8.26 kcal/mol) 具有强烈的结合亲和力.
所有化合物都符合利宾斯基的五项规则,具有有利的药理动力学特征.
分子动力学和MM-PBSA证实了稳定的配体-蛋白相互作用,F1864-0208和F1243-0200被确定为有前途的线索.

结论:

计算证据支持GroEL作为L. interrogans.的药物目标.
已识别的天然化合物可以作为新型抗勒托螺旋药物的潜在支架.
需要进一步的体外和体内研究来确认治疗疗效和安全性.

关键词:

密度函数理论密度函数理论自由能源的景观.莱普托斯皮罗斯症是什么?分子动力学模拟模拟主要组件的主要组成部分.基于结构的虚拟选.

更多相关视频

Achieving Efficient Fragment Screening at XChem Facility at Diamond Light Source

Achieving Efficient Fragment Screening at XChem Facility at Diamond Light Source

Published on: May 29, 2021

Author Spotlight: Streamlining Protein Target Prediction and Validation via Molecular Docking and CETSA

Author Spotlight: Streamlining Protein Target Prediction and Validation via Molecular Docking and CETSA

Published on: February 23, 2024

相关概念视频

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...

Ligand Binding Sites

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...