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Protein-protein Interfaces02:04

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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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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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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.
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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Mechanisms of Membrane Domain Formation00:59

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Identifying Protein-protein Interaction Sites Using Peptide Arrays
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Targeting an Interaction Between Two Disordered Domains by Using a Designed Peptide.

Guy Mayer1, Zohar Shpilt1, Shachar Bressler1

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

Chemistry (Weinheim an Der Bergstrasse, Germany)
|March 18, 2020
PubMed
Summary
This summary is machine-generated.

Researchers designed a novel peptide targeting intrinsically disordered regions (IDRs) in cancer cells. This peptide promotes cancer cell death by inhibiting protein-protein interactions, offering a new therapeutic strategy for IDR-related diseases.

Keywords:
apoptosisiASPPintrinsically disordered regionsp53peptidesprotein-protein interactions

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Peptide-based Identification of Functional Motifs and their Binding Partners
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Intrinsically disordered regions (IDRs) are crucial in disease-related protein-protein interactions.
  • The dynamic nature of IDRs presents challenges for therapeutic targeting.

Purpose of the Study:

  • To develop a peptide-based therapeutic targeting IDRs.
  • To investigate the efficacy of a designed peptide derived from the p53 linker domain against the iASPP protein in cancer cells.

Main Methods:

  • Design of a peptide (p53 LinkTer) from disordered termini of the p53 linker domain.
  • In vitro assessment of p53 LinkTer binding affinity to the iASPP RT loop and inhibition of p53-iASPP interaction.
  • Evaluation of p53 LinkTer's stability, cellular penetration, and anti-cancer effects in vitro.

Main Results:

  • The p53 LinkTer peptide binds the iASPP RT loop with high affinity and inhibits the p53-iASPP interaction.
  • p53 LinkTer exhibits enhanced stability against proteolysis.
  • The peptide effectively penetrates cancer cells, induces apoptosis, and reduces cell viability.

Conclusions:

  • Designed peptides from IDRs can effectively target partner IDRs without pre-folding.
  • p53 LinkTer demonstrates potential as a therapeutic agent for targeting IDRs in cancer.
  • This approach offers a promising strategy for developing drugs against IDR-mediated diseases.