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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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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...
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Protein Networks02:26

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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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β-Hairpin Peptidomimetics for Protein-Protein Interaction Inhibition.

Yun Li1,2, Felix M Paulussen1,2, Tom N Grossmann3,4

  • 1Department of Chemistry and Pharmaceutical Sciences, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands.

Methods in Molecular Biology (Clifton, N.J.)
|July 15, 2025
PubMed
Summary
This summary is machine-generated.

Peptide-based therapies show promise for targeting difficult protein-protein interactions (PPIs). This study explores stabilizing beta-hairpin structures to improve their effectiveness as PPI inhibitors.

Keywords:
Interstrand crosslinksPeptidomimeticProtein-protein interactionβ-hairpinβ-turnβ-turn

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Protein-protein interactions (PPIs) are vital in disease but challenging to target with traditional drugs.
  • Intracellular PPIs with large, shallow surfaces are often considered "undruggable."
  • Peptide-based approaches offer potential for PPI inhibition with improved cellular delivery.

Purpose of the Study:

  • To explore the potential of beta-sheet-derived hairpins as novel PPI inhibitors.
  • To investigate strategies for stabilizing beta-hairpins to enhance their therapeutic properties.
  • To improve binding affinity, cellular uptake, and biostability of beta-hairpin PPI inhibitors.

Main Methods:

  • Examining strategies for stabilizing beta-hairpins.
  • Focusing on beta-turn design for structural integrity.
  • Utilizing macrocyclization and crosslinking techniques for enhanced properties.

Main Results:

  • Stabilized beta-hairpins demonstrate potential for improved binding affinity.
  • Enhanced cellular uptake and biostability are achievable through stabilization strategies.
  • Cyclic and stabilized beta-hairpins offer superior properties for PPI inhibition.

Conclusions:

  • Beta-hairpin structures represent a promising, yet underexplored, class of PPI inhibitors.
  • Stabilization techniques are key to unlocking the therapeutic potential of beta-hairpins.
  • Further research into stabilized beta-hairpins could lead to new treatments for diseases involving PPIs.