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相关概念视频

Protein-Drug Binding: Mechanism and Kinetics01:16

Protein-Drug Binding: Mechanism and Kinetics

600
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,...
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Ligand Binding Sites02:40

Ligand Binding Sites

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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...
12.9K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

4.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.8K
Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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相关实验视频

Updated: Jul 20, 2025

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors
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基于LSD1的可逆抑制剂虚拟查和结合机制计算研究 计算研究

Zhili Yin1, Shaohui Liu1, Xiaoyue Yang1

  • 1School of Pharmaceutical Sciences, Zhengzhou University, Zhengzhou 450001, China.

Molecules (Basel, Switzerland)
|July 29, 2023
PubMed
概括

研究人员确定了新型的可逆抑制剂,用于基因素氨酸特异性脱甲基酶1 (LSD1),这是癌症的关键表观遗传标. 这些化合物表现出强烈的结合亲和力,为药物设计提供新的治疗策略和见解.

关键词:
这是一种LSD1抑制剂.具有约束力的自由能源计算.分子对接的分子对接.分子动力学模拟,分子动力学模拟药物学家模型的模型.虚拟选 虚拟选 虚拟选

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科学领域:

  • 生物化学 生物化学
  • 表观遗传学 在表观遗传学中,表观遗传学是指表观遗传学.
  • 药用化学 医学化学

背景情况:

  • 素基因特异性去甲基酶1 (LSD1) 是一种关键的表观遗传调节剂,与各种癌症有关.
  • 现有的不可逆转的LSD1抑制剂面临挑战,包括毒性和因酶的结合口袋特性而受到的限制.
  • 需要新的,可逆的LSD1抑制剂,具有更好的安全性和有效性.

研究的目的:

  • 确定和描述LSD1.1.的新型可逆抑制剂.
  • 探索LSD1向癌症治疗的新化学支架.
  • 为LSD1抑制剂的合理设计提供理论基础.

主要方法:

  • 采用基于结构和基于带的虚拟选策略.
  • 利用分子对接,药模拟和药物相似性评估.
  • 进行了ADMET选,分子动力学模拟和结合性自由能量计算.

主要成果:

  • 选了超过200万种化合物,确定了五种被归类为胺或1,2,4-三-4,3-α-quinazoline衍生物的成功化合物.
  • 化合物4 (Comp4) 在已识别的抑制剂中表现出最高的结合亲和力.
  • 分析显示范德瓦尔斯相互作用是主要的结合力,FAD有助于结合稳定性和减少目标外效应.

结论:

  • 该研究成功地确定了具有潜在治疗应用的新型可逆LSD1抑制剂.
  • 这些发现扩大了已知的LSD1抑制剂的化学多样性,并为合成化学家提供了新的见解.
  • 这项工作为开发更安全,更有效的LSD1向癌症治疗奠定了理论基础.