Issue 5, 2020

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

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

Supplementary files

Article information

Article type
Communication
Submitted
10 ago 2020
Accepted
09 set 2020
First published
21 set 2020
This article is Open Access
Creative Commons BY license

RSC Chem. Biol., 2020,1, 379-384

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, 1, 379 DOI: 10.1039/D0CB00146E

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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