Designing Allosteric Regulators of Thrombin. Monosulfated Benzofuran Dimers Selectively Interact With Arg173 of Exosite II to Induce Inhibition

Earlier, we reported on the design of sulfated benzofuran dimers (SBDs) as allosteric inhibitors of thrombin (Sidhu et al. (2011) J Med Chem 54: 5522-5531). To identify the site of binding of SBDs, we studied thrombin inhibition in the presence of exosite 1 and 2 ligands. Whereas hirudin peptide and...

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Detalhes bibliográficos
Main Authors: Abdel Aziz, May H., Sidhu, Preetpal Singh, Liang, Aiye, Kim, Ji Yeong, Mosier, Philip D., Zhou, Qibing, Farrell, David H., Desai, Umesh R.
Formato: Artigo
Idioma:Inglês
Publicado em: 2012
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Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3416887/
https://ncbi.nlm.nih.gov/pubmed/22788964
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jm300670q
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