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

dc.contributor.authorClayton, Daniel
dc.contributor.authorKulkarni, Sameer S.
dc.contributor.authorSayers, Jessica
dc.contributor.authorDowman, Luke J.
dc.contributor.authorRipoll Rozada, Jorge
dc.contributor.authorBarbosa Pereira, Pedro José
dc.contributor.authorPayne, Richard J.
dc.contributor.otherUniversidad de Cantabriaes_ES
dc.date.accessioned2025-11-17T11:47:22Z
dc.date.available2025-11-17T11:47:22Z
dc.date.issued2020
dc.identifier.issn2633-0679
dc.identifier.urihttps://hdl.handle.net/10902/38194
dc.description.abstractThe 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.es_ES
dc.format.extent6 p.es_ES
dc.language.isoenges_ES
dc.publisherRoyal Society of Chemistryes_ES
dc.rights© The Royal Society of Chemistry 2020. This article is licensed under a Creative Commons Attribution 3.0es_ES
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es/*
dc.sourceRSC Chemical Biology, 2020, 1, 379es_ES
dc.titleChemical synthesis of a haemathrin sulfoprotein library reveals enhanced thrombin inhibition following tyrosine sulfationes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherVersionhttps://doi.org/10.1039/d0cb00146ees_ES
dc.rights.accessRightsopenAccesses_ES
dc.identifier.DOI10.1039/d0cb00146e
dc.type.versionpublishedVersiones_ES


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