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Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
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.
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Covalent Binding of BMP-2 on Surfaces Using a Self-assembled Monolayer Approach
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Binding to protein surfaces by supramolecular multivalent scaffolds.

Vera Martos1, Pilar Castreño, Julián Valero

  • 1Institute of Chemical Research of Catalonia (ICIQ), Avda. Països Catalans 16, 43007 Tarragona, Spain.

Current Opinion in Chemical Biology
|September 20, 2008
PubMed
Summary

Artificial multivalent ligands, including scaffolds, dendrimers, and nanoparticles, are crucial for targeting biological recognition sites. These advanced materials offer promising biomedical applications by modulating protein interactions.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Nanotechnology

Background:

  • Multivalency is key in biological recognition, especially at protein-protein and protein-carbohydrate interfaces.
  • Artificial multivalent ligands are increasingly important for modulating these interactions.
  • Diverse scaffolds are being developed to mimic or interfere with natural binding events.

Purpose of the Study:

  • To review the diverse scaffolds used in developing artificial multivalent ligands.
  • To highlight the biomedical importance and applications of these ligands.
  • To discuss the advantages of various structural designs, from rigid to flexible and nanoscale.

Main Methods:

  • Review of existing literature on multivalent ligand scaffolds.
  • Categorization of ligands based on structure (e.g., calixarenes, dendrimers, rotaxanes, polymers, nanoparticles).
  • Discussion of binding affinities and biological applications.

Main Results:

  • Small molecule scaffolds (calix[4]arenes, porphyrins) can achieve nanomolar affinity.
  • Dendrimers show potential for inhibiting toxin and lectin adherence.
  • Flexible platforms (rotaxanes, polymers) and nanoparticles offer alternative design strategies.

Conclusions:

  • A wide array of multivalent scaffolds are being explored for biomedical applications.
  • Nanoparticles present significant biological and synthetic advantages for ligand development.
  • Artificial multivalent ligands are a promising area for therapeutic intervention and diagnostics.