Chemical synthesis of a haemathrin sulfoprotein library reveals enhanced thrombin inhibition following tyrosine sulfation
Literature Information
Publication Date
2020-09-21
DOI
10.1039/D0CB00146E
Impact Factor
0
Authors
Daniel Clayton, Sameer S. Kulkarni, Jessica Sayers, Luke J. Dowman, Jorge Ripoll-Rozada, Pedro José Barbosa Pereira
View Original
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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Source Journal
Recommended Compounds
Methyl 2-cyano-3,12-dioxooleana-1,9(11)-dien-28-oate
CAS Number:
218600-53-4
Molecular Formula:
C32H43NO4
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