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Related Concept Videos

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...
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...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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Related Experiment Video

Updated: Jun 23, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
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Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

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Maximising multivalency effects in protein-carbohydrate interactions.

Roland J Pieters1

  • 1Department of Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, P. O. Box 80082, 3508 TB Utrecht, The Netherlands. R.J.Pieters@uu.nl

Organic & Biomolecular Chemistry
|May 8, 2009
PubMed
Summary
This summary is machine-generated.

Multivalent carbohydrates, engineered into various structures like nanoparticles, significantly boost potency as ligands or inhibitors. This study explores optimal designs and mechanisms for enhanced carbohydrate binding effects.

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Area of Science:

  • Carbohydrate chemistry
  • Biomolecular interactions
  • Materials science

Background:

  • Multivalent carbohydrates are synthesized in diverse forms including dendrimers, polymers, nanoparticles, and nanotubes.
  • These structures aim to amplify the efficacy of carbohydrates acting as ligands or inhibitors.
  • Valency can range from two to over two thousand carbohydrate units per system.

Purpose of the Study:

  • To review popular target proteins for multivalent carbohydrate binding and inhibition.
  • To discuss optimal multivalent systems that exhibit significant multivalency effects.
  • To analyze the underlying mechanisms driving multivalent carbohydrate binding.

Main Methods:

  • Literature review and perspective synthesis.
  • Selection of key target proteins for multivalent interactions.
  • Analysis of structure-activity relationships in carbohydrate multivalency.

Main Results:

  • Diverse supramolecular architectures effectively enhance carbohydrate ligand/inhibitor potency.
  • Significant multivalency effects are observed across various valency ranges and molecular formats.
  • Specific protein targets demonstrate high affinity for multivalent carbohydrate ligands.

Conclusions:

  • Multivalent carbohydrate engineering offers a powerful strategy to enhance biological interactions.
  • Understanding the mechanisms of multivalent binding is crucial for designing effective carbohydrate-based therapeutics.
  • The choice of scaffold and valency is critical for optimizing binding potency and specificity.