Investigation of binding between myostatin and follistatin in horse and human

Document Type : Full Research Paper

Authors

1 Department of Animal Science, Faculty of Agriculture, Ferdowsi University of Mashhad, Mashhad, Iran.

2 Department of Animal Science, Faculty of Agriculture, Ferdowsi University of Mashhad, Iran

Abstract

Introduction and Aim: Inhibition of myostatin gene in animal species shows different effects. Inhibition of this gene in horses is related to running speed, and in mouse, sheep, goat and cow will increases strength and muscle mass, and reduces fat tissue. Therefore, the aim of the present study is to investigate the possibility of binding between follistatin and myostatin in horse and human through molecular docking methods. Methods: Dominant isoforms of protein sequences were obtained from the UniProt database and their structure was modeled using SWISS-MODEL server. Energy optimization was performed using the Yasara server and the quality of the models was evaluated by the Saves server. Then, the modeled structures were docked using HDock server to investigate the possibility of interaction. Four connections between human myostatin and follistatin, horse myostatin and follistatin, human myostatin and horse follistatin, and finally horse myostatin and human follistatin were investigated. Hydrogen bonds were also analyzed with Pymol and LigPlot softwares. Results: The results showed that binding between myostatin and follistatin was successfully performed in both horse and human species. Although the interaction between human myostatin and follistatin showed a greater number of hydrogen bonds, the horse intraspecific interaction produced stronger hydrogen bonds, with a more negative value. Also, in the interaction between human myostatin and horse follistatin,four common bonds with the human species were observed, which indicates the possibility of binding between these two species, where a relatively high affinity for binding was observed (docking score -308.35). Also, the interaction between horse myostatin and human follistatin was relatively strong (docking score -267.41).Structural analysis provided molecular evidence to support this possible cross-inhibition. Conclusion: The results indicated the possibility of application of human follistatin to block horse myostatin and as a result, an increase in muscle mass. This research should be validated with experimental studies.

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Veterinary Research & Biological Products
Volume 39, Issue 2
2-86
July 2026
Pages 46-56

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History

  • Receive Date: 21 October 2025
  • Revise Date: 23 December 2025
  • Accept Date: 27 December 2025

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