调试蛋白冠状体的动态:在纳米-生物接口的形成,组成,挑战和应用
Aqib Iqbal Dar1, Shiwani Randhawa1, Mohini Verma1
1Biotechnology Division, CSIR-Institute of Himalayan Bioresource Technology, Palampur, HP 176061, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.
Advances in colloid and interface science
|May 4, 2025
概括
由覆盖纳米粒子的生物分子形成的蛋白质冠状,影响其生物功能. 先进的AI/ML工具现在可以预测它的组成和效果,指导纳米医药的开发.
科学领域:
- * 纳米材料-生物分子相互作用.
- *纳米技术和生物医学应用.
背景情况:
- * 在纳米-生物接口的蛋白质冠状形成对纳米粒子行为至关重要.
- * 了解蛋白质-纳米粒子相互作用是纳米医学的关键.
- * 蛋白冠影响纳米粒子的身份和功能.
研究的目的:
- * 探索蛋白质冠状形成,组成和热力学.
- * 审查药物输送和超神术中的挑战和应用.
- *强调AI/ML在预测冠状病毒效应和指导纳米医学方面的作用.
主要方法:
- *对有关蛋白质-纳米粒子相互作用的现有文献的综述.
- * 分析影响蛋白冠状形成的因素.
- * 检查AI/ML在预测冠状病毒组成和结果方面的应用.
主要成果:
- * 蛋白质冠状体显著改变纳米粒子的生物身份和功能.
- *AI/ML工具比传统方法提高了预测准确性和效率.
- *通过纳米材料工程量身定制蛋白质冠状体,提供了新的治疗策略.
结论:
- * 蛋白冠状动力学对于纳米医学的有效性至关重要.
- *AI/ML彻底改变了蛋白质-纳米粒子相互作用的研究.
- *未来的纳米医学开发需要模拟生物环境和工程NP系统.
相关概念视频
Protein Dynamics in Living Cells
2.0K
Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
2.0K
Protein-protein Interfaces
12.4K
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...
12.4K
Protein-Protein Interfaces
3.6K
3.6K
Protein Diffusion in the Membrane
4.3K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
4.3K
Protein Folding
116.6K
Overview
116.6K
Noncovalent Attractions in Biomolecules
45.8K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
45.8K


