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February 22, 2026Physical Chemistry Chemical Physics0 citations

Triazole-stapled p53 mimetics as MDM2 inhibitors: structural and thermodynamic origin of enhanced binding affinity

VGVikram GaikwadPVPushyaraga P. VenugopalRCRajarshi Chakrabarti

Key Points

  • The aim is to investigate how triazole-stapled p53 peptides inhibit the p53-MDM2 interaction.
  • Utilized triazole-stapled peptides at specific positions (4-11) to enhance binding affinity.
  • Analyzed peptide-protein contacts and water-mediated interactions.
  • Studied the structural and thermodynamic properties of the interactions.
  • Triazole-stapled p53 peptides effectively block the p53-MDM2 interaction.
  • Stapling significantly strengthens peptide-protein contacts.
  • Enhanced binding affinity was observed due to improved water-mediated interactions.

Abstract

Triazole-stapled p53 peptides effectively block the oncogenic p53–MDM2 interaction by strengthening peptide–protein contacts and water-mediated interactions. Stapling at positions 4–11 enhances the binding affinity of p53 towards MDM2.

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Cite This Study

Gaikwad et al. (2026) studied this question.

synapsesocial.com/papers/699a9e00482488d673cd4633https://doi.org/10.1039/d5cp03813h
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