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Articles

Structural and dynamic properties of thymopoietin mimetics

, , , , , & show all
Pages 1793-1801 | Received 31 May 2013, Accepted 12 Aug 2013, Published online: 11 Sep 2013
 

Abstract

We propose a hypothesis that the T-cell receptor is a possible target of thymic hormones. We modelled the conformational dynamics of thymopentin and its structural variants in solution, as well as the interactions of these short peptides with the proposed molecular target. Thymopentin is a five-amino-acid fragment of the thymic hormone thymopoietin (residues 32 to 36) that reproduces the immunomodulatory activity of the complete hormone. Using molecular dynamics and flexible docking methods, we demonstrated high-affinity binding of thymopentin and its prospective mimetics with the T-cell receptor. The calculated biological activity spectra of thymopentin and its two promising modifications can be used in immunomodulatory activity screenings with live systems.

Acknowledgements

Authors thank Elsevier WebShop Language Service for help with language editing.

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