相关实验视频
Updated: Jul 19, 2025

07:31
Nitropeptide Profiling and Identification Illustrated by Angiotensin II
Published on: June 16, 2019
5.7K
原子分子洞察力对 ангиотензин-(1-7) 互相互作用
Luz América Chi-Uluac1,2, Somayeh Asgharpour3, Rodolfo Guadalupe Blanco-Rodríguez2,4
1Laboratory for the Design and Development of New Drugs and Biotechnological Innovation, Escuela Superior de Medicina, Instituto Politécnico Nacional, Plan de San Luis y Díaz Mirón, Ciudad de México 11340, Mexico.
Journal of chemical information and modeling
|August 17, 2023
概括
ангиотензин-(1-7) 聚是依赖pH值的,在中性pH值但不是酸性pH值形成群. 盐度也可以诱导聚合,这表明综合因素影响其物理不稳定性.
科学领域:
- 生物化学 生物化学
- 物理化学 物理化学
- 药理学 药理学是指药理学的学科.
背景情况:
- ангиотензин-(1-7) 具有显著的血管保护,抗氧化和抗炎性质.
- 它的治疗潜力受到水溶液中pH值依赖的物理不稳定性所阻碍.
- 对这种不稳定性缺乏详细的原子学理解.
研究的目的:
- 使用全原子分子动力学模拟来研究血管素-(1-7) 的聚合行为.
- 阐明pH值,离子强度和度对血管素-(1-7) 寡合化的影响.
- 提供对体物理不稳定性背后的机制的见解.
主要方法:
- 采用了全原子分子动力学模拟.
- 模拟在不同的条件下进行:酸性和中性pH值,生理和高离子强度,以及不同的度.
- 用集群分析和氨基酸相互作用图分析来解释结果.
主要成果:
- 在酸性pH条件下, ангиотензин-(1-7) 呈现出最小的集群.
- 在中性pH条件下观察到聚合成单个集群,与报告的不稳定性相关.
- 在酸性pH条件下增加盐度,导致类似于中性pH条件的聚合.
结论:
- ангиотензин-(1-7) 的类聚合是由pH和盐度的组合调节的.
- 这些发现为理解和潜在地减轻血管酶-1-7的不稳定性提供了机制基础.
- 采用的计算协议适用于研究其他系统中的互相互作用.
更多相关视频
相关概念视频
Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors
690
Angiotensin-converting enzyme (ACE), a vital component of the renin-angiotensin-aldosterone system, is abundant in lung endothelial cells. ACE converts the inactive decapeptide, angiotensin I, into the active octapeptide, angiotensin II. This potent vasoconstrictor narrows blood vessels, increasing resistance to blood flow and elevating blood pressure. Angiotensin II also stimulates aldosterone production, encouraging kidney cells to reabsorb more sodium and water from urine, thereby increasing...
690
Protein-protein Interfaces
12.5K
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...
12.5K
Antihypertensive Drugs: Angiotensin II Receptor Blockers
780
In the renin-angiotensin-aldosterone system, a hormone called angiotensin II plays a crucial role. It binds to the AT1 receptors in vascular smooth muscles coupled with Gq proteins. The activation of these receptors activates an enzyme called phospholipase C, which releases two molecules: inositol trisphosphate and diacylglycerol. These molecules cause a chain reaction that leads to the phosphorylation of myosin light chains and promotes interaction between actin and myosin, leading to smooth...
780
Antihypertensive Drugs: Direct Renin Inhibitors
680
The renin-angiotensin-aldosterone system (RAAS) is an intricate physiological pathway involving numerous enzymes and hormones, including renin, angiotensin-converting enzyme (ACE), angiotensin I and II, and aldosterone. Imbalances within this system increase the production of angiotensin II and aldosterone. Increased angiotensin II levels promote vasoconstriction and blood pressure elevation. Concurrently, higher aldosterone levels stimulate sodium and water reabsorption in the kidneys,...
680
Protein Organization
6.6K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
The primary structure of a protein is its amino acid sequence....
6.6K
Peptide Bonds
74.8K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
74.8K

