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Related Concept Videos

Protein Folding01:25

Protein Folding

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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...

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Related Experiment Video

Updated: Jun 6, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

Stabilizing the eIF4G1 α-helix increases its binding affinity with eIF4E: implications for peptidomimetic design

C J Brown1, J J Lim, T Leonard

  • 1p53 Lab (p53Lab), 8A Biomedical Grove, #06-06, Immunos, Singapore 138648. cjbrown@p53lab.a-star.edu.sg

Journal of Molecular Biology
|November 25, 2010
PubMed
Summary

Researchers developed a stabilized peptide targeting eukaryotic initiation factor 4E (eIF4E), overexpressed in cancers. This novel peptide effectively inhibits cancer-promoting protein translation and induces cancer cell death, offering a promising therapeutic strategy.

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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
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Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Related Experiment Videos

Last Updated: Jun 6, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

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Published on: May 1, 2020

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Therapeutics

Background:

  • Eukaryotic initiation factor 4E (eIF4E) overexpression is common in various cancers, promoting tumor growth by enhancing translation of oncogenic proteins.
  • Targeting eIF4E presents a potential therapeutic strategy for human cancers.
  • Existing eIF4E inhibitors lack sufficient potency or biological activity.

Purpose of the Study:

  • To design and synthesize a novel, helically stabilized peptide targeting eIF4E.
  • To evaluate the binding affinity, potency, and biological activity of the stabilized peptide.
  • To assess the therapeutic potential of cell-penetrating peptide-fused derivatives in cancer models.

Main Methods:

  • Peptide synthesis based on the eIF4G1 binding motif with stabilized α-helix.
  • Circular dichroism (CD) measurements to confirm α-helix stabilization.
  • Binding affinity (K(d)) determination, cell-based cap-dependent translational reporter assays, WST-1 assays for cell metabolism, propidium iodide and Annexin V staining for cell death analysis.

Main Results:

  • The helically stabilized peptide exhibited significantly higher binding potency (K(d) of 9.43±2.57 nM) compared to the template peptide.
  • The stabilized peptide demonstrated significant biological activity in cell-based assays at 400 μM, unlike the template peptide.
  • TAT-fused stabilized peptides effectively inhibited cap-dependent translation, induced significant cell death via apoptosis, and reduced G1/G2 cell populations.

Conclusions:

  • Helically stabilized peptidomimetics targeting eIF4E are potent inhibitors of cap-dependent translation.
  • TAT-fusion enhances cellular uptake and efficacy, leading to apoptosis in cancer cells.
  • These findings provide a strong foundation for developing novel peptidomimetic-based cancer therapeutics targeting eIF4E.