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Related Concept Videos

The Two-State Receptor Model01:29

The Two-State Receptor Model

The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...
Spare Receptors01:30

Spare Receptors

Some receptors remain unoccupied even when an agonist produces a maximal response. Such empty ones are called spare receptors. In presence of spare receptors the maximum effect of an agonist drug is achieved with fewer than 100% of the receptors being occupied. To determine the presence of spare receptors, scientists often compare the concentration of the drug needed to produce 50% of the maximum effect (EC50) with the concentration of the drug needed to occupy 50% of the receptors (Kd). If the...
Quantitative Aspects of Drug-Receptor Interaction01:30

Quantitative Aspects of Drug-Receptor Interaction

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 Kd...
Drug-Receptor Interactions01:29

Drug-Receptor Interactions

Drug-receptor interaction describes the binding of receptors by drugs, but not all drug-receptor interactions result in activation and tissue response. For instance, the binding of agonists activates the receptor to generate a cellular reaction, while antagonists bind to receptors without causing their activation.
Several parameters, such as the drug's affinity for its receptor and its efficacy, which is its ability to activate the receptor, determine the drug's effect on the tissue.
Drug-Receptor Interaction: Agonist01:25

Drug-Receptor Interaction: Agonist

Agonists are drugs that interact with specific receptors in the body to produce a biological response. When an agonist binds to a receptor, it activates or enhances the receptor's function, leading to physiological effects. The interaction between agonist drugs and receptors is crucial for their therapeutic action in various medical treatments.
Agonists can bind to receptors in different ways. Some agonists bind directly to the receptor's active site, mimicking the endogenous ligand's action.
Dose-Response Relationship: Overview01:03

Dose-Response Relationship: Overview

Agonists can bind with and activate receptors, resulting in the formation of drug-receptor complexes. Once formed, these complexes catalyze many biochemical processes at the cellular level and subsequently induce a pharmacologic response. The degree of response is directly proportional to the fraction of activated receptors, which in turn, depends on the concentration of the drug at the receptor site as well as the sensitivity of the receptor. An increase in the administered dose contributes to...

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High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy
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High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy

Published on: July 25, 2014

Maximum likelihood and the single receptor.

Robert G Endres1, Ned S Wingreen

  • 1Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, United Kingdom. r.endres@imperial.ac.uk

Physical Review Letters
|November 13, 2009
PubMed
Summary
This summary is machine-generated.

Biological cells sense chemical concentration with accuracy limited by particle diffusion. This study derives a new lower limit by analyzing unoccupied receptor intervals, improving concentration estimation accuracy.

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Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

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Area of Science:

  • Biophysics
  • Cellular Biology
  • Physical Chemistry

Background:

  • Cellular sensing of chemical concentrations is crucial for biological processes.
  • The Berg-Purcell limit, based on diffusion and random particle arrival, is the established physical accuracy limit.
  • Current models do not fully account for how receptor states influence sensing accuracy.

Purpose of the Study:

  • To derive a more accurate lower limit for cellular chemical sensing.
  • To investigate the role of receptor occupancy time intervals in determining sensing accuracy.
  • To propose optimal cellular sensing strategies based on physical principles.

Main Methods:

  • Applied maximum likelihood estimation to time series of receptor occupancy.
  • Analyzed unoccupied receptor intervals to extract information about external particle concentration.
  • Developed a theoretical framework for optimal receptor-ligand dynamics.

Main Results:

  • Derived a novel lower bound for sensing accuracy, surpassing the Berg-Purcell limit under specific conditions.
  • Demonstrated that unoccupied receptor intervals contain the primary information about external concentration.
  • Showed that occupied intervals decrease the accuracy of concentration estimation.
  • Identified receptor strategies that minimize bound time intervals for maximal accuracy.

Conclusions:

  • A more precise physical limit for cellular chemical sensing has been established.
  • Optimal cellular sensing involves focusing on unoccupied receptor intervals and minimizing bound particle durations.
  • Cells can achieve higher sensing accuracy by actively managing bound particles, e.g., through absorption or degradation.