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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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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Side-Chain Engineering Guides the Design of β-Sheet Inhibitor to Anchor Protein-Protein Interaction Interfaces.

Limin Zhang1, Minxuan Wang1, Bo Wang1

  • 1Key Laboratory of Medical Molecule Science and Pharmaceutics Engineering, Ministry of Industry and Information Technology, Key Laboratory of Cluster Science of Ministry of Education, Beijing Key Laboratory of Photoelectronic/Electro-photonic Conversion Materials, School of Chemistry and Chemical Engineering, Tangshan Research Institute, Beijing Institute of Technology, Beijing, 100081, P.R. China.

Angewandte Chemie (International Ed. in English)
|January 7, 2026
PubMed
Summary

Designing stable beta-sheet inhibitors for protein-protein interactions (PPIs) is now feasible. A new amino acid side-chain engineering strategy (AASE) creates effective beta-sheet structures for tumor imaging and therapy.

Keywords:
PD‐L1Protein‐protein interactions (PPIs)Targeting peptideβ‐sheet inhibitors

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Area of Science:

  • Medicinal Chemistry
  • Biochemistry
  • Molecular Biology

Background:

  • Developing inhibitors for beta-sheet mediated protein-protein interactions (PPIs) is challenging.
  • Peptides often lose secondary structure, reducing affinity.
  • Stable beta-sheet inhibitor design lacks reliable strategies.

Purpose of the Study:

  • To propose a novel amino acid side-chain engineering strategy (AASE) for designing stable beta-sheet inhibitors.
  • To guide the design of beta-sheet backbones using amino acid pairing (AAP) and non-covalent interactions.
  • To generate and validate structurally defined beta-sheet inhibitors for therapeutic applications.

Main Methods:

  • Amino acid side-chain engineering strategy (AASE) based on amino acid pairing (AAP) principle.
  • Integration of complementarity of non-covalent interactions between beta-strand side chains.
  • High-throughput peptide screening and validation of physicochemical properties.

Main Results:

  • AASE successfully generated structurally defined beta-sheet inhibitors.
  • Prioritized peptide EH demonstrated potent biological functions.
  • EH enabled high-resolution tumor imaging and PD-1/PD-L1 checkpoint blockade therapy.

Conclusions:

  • The AASE provides a reliable method for designing stable beta-sheet inhibitors.
  • EH shows promise for tumor imaging, surgical guidance, and cancer immunotherapy.
  • This strategy offers valuable insights for future PPI inhibitor development.