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

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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.

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

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Supplementary files

Article information


Submitted
10 Aug 2020
Accepted
09 Sep 2020
First published
21 Sep 2020

This article is Open Access

RSC Chem. Biol., 2020, Advance Article
Article type
Communication

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

D. Clayton, S. S. Kulkarni, J. Sayers, L. J. Dowman, J. Ripoll-Rozada, P. J. B. Pereira and R. J. Payne, RSC Chem. Biol., 2020, Advance Article , DOI: 10.1039/D0CB00146E

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