An update on recent patents on thrombin inhibitors (2010 – 2013)

@article{Mehta2014AnUO,
  title={An update on recent patents on thrombin inhibitors (2010 – 2013)},
  author={Akul Y. Mehta and Yingzi Jin and Umesh R. Desai},
  journal={Expert Opinion on Therapeutic Patents},
  year={2014},
  volume={24},
  pages={47 - 67}
}
Introduction: Thromboembolic incidences have increased nearly 33% in the past decade and directly affect nearly 0.5% of the population. Heparin, warfarin and current direct thrombin inhibitors (DTIs), the primary anticoagulants of choice, suffer from several drawbacks. Thus, the search for an antithrombotic devoid of adverse effect continues in earnest. Areas covered: Literature search covering PubMed, SciFinder™ Scholar, Web of Knowledge, Espacenet, PatentScope and Google Patent Search was… 
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This review summarizes the development of orally active thrombin inhibitors for the treatment of thrombotic disorder diseases, which could serve as a reference for the interested researchers.
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The results suggest that two new anticoagulant peptides (Z‐YQQ and YQQ) can be useful for safe pharmaceutical applications, Nevertheless, some aspects related to peptide production should be optimized.
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Amaranth peptides with antithrombotic activity released by simulated gastrointestinal digestion
Modulating hydrogen-bond basicity within the context of protein-ligand binding: A case study with thrombin inhibitors that reveals a dominating role for desolvation.
Antithrombotic Activity of Milk Protein Hydrolysates by Lactic Acid Bacteria Isolated from Commercial Fermented Milks
In the last decade, thrombosis has been one of the pathologies with high incidence creating great concern in Health Institutes all around the world. Considering this, the aim of this research was to…
Rapid magnetic solid-phase extraction combined with ultra-high performance liquid chromatography and quadrupole-time-of-flight mass spectrometry for analysis of thrombin binders from a crude extract and injection of Erigeron breviscapus
Thrombin, which acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, plays crucial roles in the blood coagulation pathway. Inhibition of thrombin leading to…
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