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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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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.
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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Identifying Protein-protein Interaction Sites Using Peptide Arrays
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Targeting Protein Interaction Hotspots Using Structured and Disordered Chimeric Peptide Inhibitors.

Guy Mayer1, Zohar Shpilt1, Hadar Kowalski1

  • 1The Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus, Givat Ram, Jerusalem 9190401, Israel.

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Designing chimeric peptides effectively inhibits protein-protein interactions (PPIs) by targeting both structured and disordered regions. This novel approach shows promise for developing new cancer therapeutics.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Protein-protein interactions (PPIs) are crucial in cellular processes, but their therapeutic inhibition is challenging.
  • Targeting interaction hotspots, which can be structured or disordered, requires innovative molecular design.

Purpose of the Study:

  • To develop a strategy for inhibiting both structured and disordered interaction hotspots using chimeric peptides.
  • To create peptide inhibitors targeting the antiapoptotic iASPP protein, a relevant target in cancer therapy.

Main Methods:

  • Designed and synthesized chimeric peptides combining cyclic structured and disordered elements.
  • Developed a structured, α-helical stapled peptide inhibitor targeting iASPP.
  • Created chimeric peptides by linking structured and disordered peptide components.

Main Results:

  • The structured peptide inhibitor bound iASPP hotspots and exhibited cytotoxicity in A2780 cancer cells (IC50 = 10 ± 1 μM).
  • Chimeric peptides demonstrated higher affinity for iASPP than individual peptides, targeting both structured and disordered domains.
  • The developed chimeric peptides induced cancer cell death.

Conclusions:

  • Chimeric peptides offer a viable strategy to overcome challenges in inhibiting PPIs involving both structured and disordered protein regions.
  • This approach broadens the interface targeted by inhibitors, enhancing their efficacy.
  • The findings support the development of chimeric peptide inhibitors for therapeutic applications, particularly in cancer treatment.