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相关概念视频

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

12.9K
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-Drug Binding: Determination Methods01:22

Protein-Drug Binding: Determination Methods

196
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...
196
Ligand Binding Sites02:40

Ligand Binding Sites

12.9K
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...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Quantitative Aspects of Drug-Receptor Interaction01:30

Quantitative Aspects of Drug-Receptor Interaction

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The receptor occupancy theory connects a drug's response to the number of occupied receptors. With higher drug concentrations, more receptors are occupied, leading to increased responses. The formation of drug-receptor complexes involves association and dissociation rates, which reach equilibrium when the forward and backward reactions are equal. The equilibrium association constant (Ka) and its inverse, the equilibrium dissociation constant (Kd), indicate drug affinity. Higher Ka and lower...
997
Drug-Receptor Bonds01:25

Drug-Receptor Bonds

2.8K
Drug-receptor bonds are formed through various chemical forces when drugs interact with target cells. Covalent bonds, strong and irreversible, are exemplified by DNA-alkylating anticancer agents that inhibit cell division. However, such irreversible drug binding lacks selectivity and can modify the DNA of the surrounding healthy cells. Covalent binding often contributes to tissue toxicity, as seen with chloroform and paracetamol metabolites binding to the liver, causing hepatotoxicity.
In...
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相关实验视频

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An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions
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An ELISA Based Binding and Competition Method to Rapidly Determine Ligand-receptor Interactions

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直接结合的方法来测量受体-质体相互作用.

Manisha Ray1, Aryana Sayeed1, Madeline Ganshert1

  • 1Department of Chemistry and Biochemistry, Loyola University Chicago, 1068 W. Sheridan Road, Chicago, Illinois 60660, United States.

The journal of physical chemistry. B
|December 22, 2023
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概括

这项研究引入了一种新的无标签,自由溶液方法来测量G蛋白结合受体 (GPCR) 相互作用. 该技术量化了近本地条件的直接结合亲缘关系,推动了GPCR药物发现.

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Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR
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Fluorescence Biomembrane Force Probe: Concurrent Quantitation of Receptor-ligand Kinetics and Binding-induced Intracellular Signaling on a Single Cell
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科学领域:

  • 生物化学 生物化学
  • 药理学 药理学是指药理学的学科.
  • 生物物理学的生物物理.

背景情况:

  • G蛋白结合受体 (GPCRs) 对生理过程至关重要,使其成为关键药物标.
  • 目前对GPCR的间接测定缺乏直接结合测量,阻碍了药物发现.
  • 现有的直接方法经常使用标签或为受体创建非原生环境.

研究的目的:

  • 开发一种无标签,无固定化技术,用于测量GPCR-连接物相互作用.
  • 在接近原生条件下量化直接结合亲和力和动力学.
  • 克服间接信号测定和传统直接结合方法的局限性.

主要方法:

  • 使用基于属性的自由解法技术,使用折射率 (RI).
  • 在没有受体固定或标签的情况下测量了结合相互作用.
  • 在复杂的细胞环境中应用该方法来量化生物活性脂质和相关脂质GPCR之间的相互作用.

主要成果:

  • 通过使用开发的自由溶液方法,成功量化了生物活性脂质与脂质GPCRs的相互作用.
  • 证明了在接近原生条件下测量结合的能力,包括其他细胞质脂质和蛋白质.
  • 验证了一种无标签的方法,可以绕过受体固定.

结论:

  • 开发的自由溶液技术提供了一个强大的无标签方法,用于研究GPCR-连接物相互作用.
  • 与传统测试相比,这种方法提供了更多与生理相关的结合性数据.
  • 鼓励在多种不同的受体-连接体对中进一步应用,以探索这种技术在生物分子相互作用研究中的全部潜力.