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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.
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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Different monodentate and polydentate ligands are used as complexing agents in complexometric titration reactions. The formation of complexes by mono- and bidentate ligands involves two or more intermediate steps, limiting their use as complexing agents. In comparison, polydentate ligands can form complexes with metal ions in a single-step process, facilitating sharper end points. This means polydentate ligands, such as amino carboxylic acid derivatives, are most commonly employed in...
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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...
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Engineering Antiviral Agents via Surface Plasmon Resonance
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Precipitation-free high-affinity multivalent binding by inline lectin ligands.

Philipp Rohse1, Sabrina Weickert1, Malte Drescher1

  • 1University of Konstanz, Department of Chemistry, Konstanz Research School Chemical Biology (KoRS-CB) Universitätsstraße 10 78457 Konstanz Germany mail@valentin-wittmann.de.

Chemical Science
|June 14, 2021
PubMed
Summary
This summary is machine-generated.

We designed novel multivalent ligands with high binding affinity that prevent receptor precipitation. This new inline design avoids plaque formation, offering potential for therapeutic applications.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Multivalent ligand-protein interactions are crucial in biological processes like signaling and adhesion.
  • High binding affinities of multivalent ligands can lead to receptor crosslinking and precipitation, causing diseases and limiting therapeutic use.

Purpose of the Study:

  • To develop a novel design for high-potency multivalent ligands that exhibit strong binding affinities.
  • To prevent receptor precipitation and associated pathological effects, enabling potential therapeutic applications.

Main Methods:

  • Design and synthesis of inline multivalent ligands with high-affinity epitopes.
  • Multi-methodological approach to analyze binding modes and receptor interactions.
  • Investigation of a unique chelating binding mode involving simultaneous bridging of four receptor sites.

Main Results:

  • Developed high-potency multivalent ligands with binding affinities in the low nanomolar range.
  • Demonstrated prevention of receptor precipitation using a multi-methodological approach.
  • Elucidated a unique chelating binding mode where one ligand bridges four receptor sites.

Conclusions:

  • The novel inline design of multivalent ligands overcomes precipitation issues associated with traditional designs.
  • This design strategy shows significant potential for developing potent multivalent inhibitors for therapeutic use.
  • The established concept is validated using the model lectin wheat germ agglutinin.