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Related Concept Videos

Ligand Binding Sites02:40

Ligand Binding Sites

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...
Ligand Binding Sites02:40

Ligand Binding Sites

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...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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 the...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

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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Modulation of Tau Subcellular Localization as a Tool to Investigate the Expression of Disease-related Genes
09:12

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Published on: December 20, 2019

Ligand electronic properties modulate tau filament binding site density.

Katryna Cisek1, Jordan R Jensen, Nicolette S Honson

  • 1Department of Molecular and Cellular Biochemistry, The Ohio State University College of Medicine, Columbus, OH 43210, USA.

Biophysical Chemistry
|October 18, 2012
PubMed
Summary

Researchers explored how molecular polarizability affects binding to tau aggregates in neurodegenerative diseases. Highly polarizable molecules effectively bind to high-density sites on tau, suggesting potential for improved Alzheimer

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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein

Published on: January 2, 2015

Area of Science:

  • Neurodegenerative diseases
  • Molecular imaging and therapeutics
  • Biochemistry of protein aggregation

Background:

  • Tau pathology is central to Alzheimer's disease and other tauopathies.
  • Developing diagnostic and therapeutic agents targeting tau requires understanding binding characteristics.
  • Molecular polarizability has been identified as a key factor in binding affinity to protein aggregates.

Purpose of the Study:

  • To investigate the role of molecular polarizability in the binding site density (B(max)) of tau aggregates.
  • To compare the binding of two benzothiazole derivatives with differing polarizabilities to tau lesions.
  • To correlate molecular structure with binding performance for improved tau-directed agent design.

Main Methods:

  • Synthesis and characterization of two benzothiazole derivatives with varying polarizability.
  • Competitive binding assays using Thioflavin S and radiolabeled IMSB as probes for tau binding sites.
  • Quantum chemical calculations to analyze electronic properties and pi-electron delocalization.

Main Results:

  • The highly polarizable benzothiazole derivative effectively displaced high-density probes (Thioflavin S).
  • Lower polarizability benzothiazole derivatives primarily displaced low-density probes (IMSB).
  • Extensive pi-electron delocalization, indicated by high polarizability, correlates with binding to high-density tau sites.

Conclusions:

  • Molecular polarizability, specifically pi-electron delocalization, is crucial for targeting high-density binding sites on tau aggregates.
  • Optimizing ligand polarizability can enhance the diagnostic and therapeutic efficacy of tau-directed agents for neurodegenerative diseases.
  • This study provides a framework for designing more effective small molecules for Alzheimer's disease and other tauopathies.