English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Thrombosis is characterized by the formation of clots in the blood vessels. Antithrombin-III deficiency in the blood causes thrombus formation. Supplementing antithrombin-III may serve as anticoagulant therapy. In the present studies, an antithrombin like Protein from  Punica granatum  has been identified and characterized using  in silico  approach. Based on sequence homology, an ALPP was selected depending upon its highest binding affinity of −41.28 kcal/mol with thrombin. Thrombin structure complexed with ALPP was docked with TAME using AutoDock Vina. No binding was observed for TAME at Ser 195  of thrombin. MD simulation (50 ns) was performed to evaluate the flexibility and stability of docked complexes.  In vitro  assays with crude protein showed 78% thrombin inhibition at 5 µg and calculated IC 50  value was 0.188 µg. The presence of thrombin inhibitors in crude protein was also confirmed by reverse zymography. Thus, it is very likely that the protein identified from  P. granatum  may act as thrombin inhibitor.

natural product research

Identification of thrombin inhibiting antithrombin-III like protein from  Punica granatum  using  in silico  approach and in vitro validation of thrombin inhibition activity in crude protein