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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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Predicted IL-18/IL-18R Binding Improvement Through Protein Interface Modification with Computer-Aided Design.

Napat Prompat1,2, Chariya Peeyatu1, Jirakrit Saetang3

  • 1Department of Biomedical Sciences and Biomedical Engineering, Faculty of Medicine, Prince of Songkla University, Songkhla 90110, Thailand.

Biomolecules
|October 29, 2025
PubMed
Summary

Computational methods were used to design mutations that enhance Interleukin-18 (IL-18) activity for cancer immunotherapy. These designed mutations show potential for improving IL-18

Keywords:
cytokine-mediated immunotherapyinterleukin-18molecular dynamics simulationstructure-guided design

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Area of Science:

  • Biochemistry and Molecular Biology
  • Immunology
  • Computational Biology

Background:

  • Cytokine immunotherapy, particularly using Interleukin-18 (IL-18), is a promising cancer treatment strategy.
  • IL-18 enhances anti-tumor responses by boosting natural killer (NK) and cytotoxic T cell activity.
  • Optimizing IL-18's interaction with its receptor is key to enhancing its therapeutic efficacy.

Purpose of the Study:

  • To computationally design and predict mutations that increase the biological activity of IL-18.
  • To investigate the effects of specific mutations on IL-18's receptor binding and stability.
  • To explore a computer-aided design approach for developing more potent IL-18-based cancer therapies.

Main Methods:

  • Structure-based computational energy calculations were employed to identify potential mutations.
  • Molecular dynamic (MD) simulations were used to assess the stability and conformational changes of mutated IL-18.
  • Analysis focused on electrostatic interactions and flexibility in key protein regions.

Main Results:

  • Four candidate mutations (E6M, E6M+N111S+R131G, E6M+K129M+R131G, E6M+N111S+K129M+R131G) were predicted to enhance IL-18 receptor binding and stability.
  • MD simulations indicated that mutations did not compromise overall protein stability but increased flexibility in the β8-β9 hairpin loop.
  • The dynamic behavior of mutated IL-18 suggests potential for improved biological activity.

Conclusions:

  • Computer-aided design is an effective strategy for enhancing IL-18 cytokine potency.
  • The identified mutations offer a basis for developing improved IL-18 variants for cancer immunotherapy.
  • Further simulations of the full IL-18-receptor complex are needed to fully validate these findings.