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September 10, 2025Communications ChemistryOpen Access

Cardiolipin acyl chain composition tailors the conformation of mammalian ATP synthase dimers

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Authors

MMMarcin MakowskiVAVíctor G. Almendro‐VediaILIván López‐Montero

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Overview

Molecular dynamics simulations reveal altered lipid influence on ATP synthase in Barth syndrome, suggesting consequences for mitochondrial function.

Key Points

  • Altered cardiolipin composition affects ATP synthase dimer conformations, impacting mitochondrial function.
  • Molecular dynamics simulations show that less unsaturated cardiolipin in Barth syndrome reduces ATP synthase dimer stability.
  • Findings highlight that lipid heterogeneity and strain modify ATP synthase conformation and efficiency of energy production.
  • This research sheds light on mitochondrial architecture and function disruptions in diseases like Barth syndrome.

Cite This Study

Makowski et al. (2025) studied this question.

synapsesocial.com/papers/68c19f9c54b1d3bfb60db174https://doi.org/10.1038/s42004-025-01611-1
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  1. 1Cardiolipin clustering promotes mitochondrial membrane dynamics2024 · 5 citations
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  3. 3P002: Exploring the role of cardiolipin metabolism in the brain through the lens of Barth syndrome and cardiolipin synthase deficiency*2026
  4. 4Role of cardiolipin alterations in mitochondrial dysfunction and disease2006 · 651 citations
  5. 5Cardiolipin dynamics promote membrane remodeling by mitochondrial OPA12025