Issue 5, 2020
From the journal:

RSC Chemical Biology

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

Daniel Clayton,a   Sameer S. Kulkarni,a   Jessica Sayers,a   Luke J. Dowman,a   Jorge Ripoll-Rozada, ORCID logo b   Pedro José Barbosa Pereira ORCID logo b  and  Richard J. Payne ORCID logo *ac  

* Corresponding authors

a School of Chemistry, The University of Sydney, Sydney, NSW 2006, Australia
E-mail: richard.payne@sydney.edu.au

b IBMC – Instituto de Biologia Molecular e Celular & Instituto de Investigação e Inovação em Saúde, Universidade do Porto, 4200-135 Porto, Portugal

c Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Sydney, Sydney, NSW 2006, Australia

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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Article information

DOI
https://doi.org/10.1039/D0CB00146E
Article type
Communication
Submitted
10 août 2020
Accepted
09 sept. 2020
First published
21 sept. 2020
This article is Open Access
Creative Commons BY license

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

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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

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