Chemical synthesis of a haemathrin sulfoprotein library reveals enhanced thrombin inhibition following tyrosine sulfation

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URI: https://hdl.handle.net/10902/38194
ISSN: 2633-0679
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Autoría
Clayton, Daniel; Kulkarni, Sameer S.; Sayers, Jessica; Dowman, Luke J.; Ripoll Rozada, Jorge; Barbosa Pereira, Pedro José; Payne, Richard J.
Fecha
2020
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© The Royal Society of Chemistry 2020. This article is licensed under a Creative Commons Attribution 3.0
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RSC Chemical Biology, 2020, 1, 379
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Royal Society of Chemistry
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Resumen/Abstract
The haemathrins are tick-derived thrombin-inhibiting proteins predicted to be post-translationally sulfated. This study reports the ligation-based assembly of eight homogeneously sulfated variants of haemathrin-1 and haemathrin-2. Functional assays revealed a two orders-of-magnitude enhancement in thrombin-inhibitory potency by tyrosine sulfation, thus reinforcing the crucial role of this post-translational modification for the activity of anticoagulant proteins.
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© The Royal Society of Chemistry 2020. This article is licensed under a Creative Commons Attribution 3.0Excepto si se señala otra cosa, la licencia del ítem se describe como © The Royal Society of Chemistry 2020. This article is licensed under a Creative Commons Attribution 3.0