关于enalapril maleate电荷转移的研究:从固态到分子动态
Ana Carolina M Lourenço1, Lauriane G Santin2, James O Fajemiroye2,3
1Grupo de Química Teórica E Estrutural de Anápolis, Universidade Estadual de Goiás, Anápolis, GO, Brazil.
Journal of molecular modeling
|June 2, 2023
概括
马莱酸盐成分影响埃纳拉普利马莱酸盐的稳定性. 一个分散的原子通过电荷转移促进了分解,而一个集中的原子提高了这种抗高血压药物的稳定性.
科学领域:
- 固态化学 固态化学
- 计算化学是一种计算化学.
- 制药科学 制药科学 制药科学
背景情况:
- 甲酸是一种抗高血压药物,存在两种晶体形式.
- 键显著影响固态稳定性,电荷转移和不同环境条件下的埃纳拉普里尔酸盐的降解.
研究的目的:
- 为了研究酸盐成分对伊纳拉普利酸盐结构稳定性的影响.
- 为了阐明结和质子转移在埃纳拉普利 Maleate 的降解和稳定机制中的作用.
主要方法:
- 使用赫什菲尔德表面和CrystalExplorer17.的超分子排列分析.
- 原子在分子中的量子理论 (QTAIM) 用于电子结构计算.
- 卡尔-帕里内洛分子动力学模拟研究质子 (H+) 电荷转移和运动.
主要成果:
- N1-H∙∙∙O7相互作用表现出部分共价性特征.
- 分子动力学揭示,在酸盐上分散的能通过电荷转移驱动分解,而集中的能则促进稳定.
- 埃纳拉普利和马莱酸盐分子之间的电荷转移和质子流动性得到证实.
结论:
- 酸盐部分内的原子的位置极大地决定了埃纳拉普利酸盐的稳定性.
- 了解这些相互作用对于控制固态稳定性和预测埃纳拉普利 Maleate 的降解途径至关重要.
关键词:
在CPMD中,您可以使用CPMD.收费转移是指收费转移的情况.埃纳拉普利尔马莱酸是什么意思希尔什菲尔德的表面表面M06-2X 6311 + + G** 6311 + + G** G06-2X 6311 + + G** G06-2X 6311 + + G** G06-2X 6311 + + G** G06-2X 6311 + + + G** G06-2X 6311 + + G06-2X 6311 + + G06-2X 6311 + + G06-2X 6311 + + G06-2X 6311 + G06-2X 6311 + G06-2X 6311 + G06-2X 6311 + G06-2X 6311 + + G06-2X 66 + G06-2X 66 + G06-2X更多相关视频
08:15Author Spotlight: Network Pharmacology and Molecular Docking to Decipher the Action of Jiawei Shengjiang San Against Diabetic Kidney Disease
Published on: May 10, 2024
614
10:29Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors
Published on: May 9, 2025
1.3K
相关概念视频
01:16Protein-Drug Binding: Mechanism and Kinetics
668
Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...
668
01:22Protein-Drug Binding: Determination Methods
248
Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...
248