蛋白质纳米生物活性剂对抗微重力诱导的内皮功能障碍
Anisha Kabir1, Mukilarasi B1, Anagha Manohar1
1Department of Applied Mechanics and Biomedical Engineering, Indian Institute of Technology Madras, Chennai, Tamil Nadu, India.
NPJ microgravity
|February 2, 2026
概括
由于微重力,宇航员在太空中面临血管功能障碍. 在模拟的太空条件下,一种新的纳米治疗 (ZNT) 配方有效地对抗氧化压力,并保护心血管健康.
科学领域:
- 太空医学 太空医学
- 纳米技术纳米技术
- 心血管研究的心血管研究.
背景情况:
- 长时间的太空任务会诱导微重力和宇宙辐射暴露,通过氧化应激和心脏脱节导致宇航员血管功能障碍.
- 目前用于太空飞行引起问题的治疗方法受到副作用的限制,并且对氧化和内皮损伤缺乏有效性.
研究的目的:
- 开发和评估一种基于多功能或纳米的治疗配方 (ZNT),用于减轻氧化应激和保护心血管健康在模拟微重力条件下.
主要方法:
- 在实验室中对暴露在模拟微重力下的内皮细胞进行研究,以评估氧化应激标志物,线粒体功能,DNA损伤,亡和血管性基因表达.
- 使用斑马鱼幼虫和小胚胎模型进行体内验证,以确认ZNT.的治疗作用.
- ZNT的配方封装了一个针对氧化应激和内皮保护的补救尾酒.
主要成果:
- 微重力诱导了显著的活性氧物种生成,线粒体功能障碍,DNA损伤和内皮细胞的亡.
- 采用ZNT治疗有效地恢复了氧化还原平衡,保持了线粒体的完整性,防止了DNA损伤和亡,并使关键血管新生基因 (VEGFA,HIF-1α,eNOS,iNOS,FGF-2,ANG1) 的表达正常化.
- 在体内证实了ZNT的保护作用,证明了它在复杂的生物系统中的有效性.
结论:
- 基于多功能和纳米的治疗配方 (ZNT) 在抵消微重力诱导的心血管损伤方面显示出显著的前景.
- ZNT解决了氧化应激和病态血管生成,为宇航员医疗提供了一种新的纳米治疗策略.
- 这种配方可以填补在太空飞行期间和之后保护宇航员心血管功能的关键缺口.
相关概念视频
2° Amines to N-Nitrosamines: Reaction with NaNO2
5.5K
Secondary amines react with nitrous acid to form N-nitrosamines, as depicted in Figure 1. Nitrous acid, a weak and unstable acid, is formed in situ from an aqueous solution of sodium nitrite and strong acids, such as hydrochloric acid or sulfuric acid, in cold conditions. In the presence of an acid, the nitrous acid gets protonated. The subsequent loss of water results in the formation of the electrophile known as nitrosonium ion.
5.5K
Protein-protein Interfaces
14.7K
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...
14.7K
Protein and Protein Structure
87.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
87.6K
Induced-fit Model
89.2K
Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
89.2K
Conservation of Protein Domains Over Different Proteins
14.5K
Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.5K
Intrinsically Disordered Proteins
19.5K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
19.5K


