For Publishers
DiscoveryMetadataPeer reviewHostingPublishing
For Researchers
JoinPublishReviewCollect
Register
Blog
About
Search
Advanced search
My ScienceOpen
Search
For Publishers
For Researchers
Blog
About
52
views
54
references
 Top references
cited by
22
    
0 reviews
 Review
0
comments
 Comment
0
recommends
+1 Recommend
1 collections
    0
    shares
      476
      similar
       All similar
      • Record: found
      • Abstract: found
      • Article: not found

      Computational study of pomegranate peel extract polyphenols as potential inhibitors of SARS-CoV-2 virus internalization

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The search for effective coronavirus disease (COVID-19) therapy has attracted a great deal of scientific interest due to its unprecedented health care system overload worldwide. We have carried out a study to investigate the in silico effects of the most abundant pomegranate peel extract constituents on the multi-step process of serious acute respiratory syndrome coronavirus 2 (SARS-CoV-2) internalization in the host cells. Binding affinities and interactions of ellagic acid, gallic acid, punicalagin and punicalin were studied on four selected protein targets with a significant and confirmed role in the process of the entry of virus into a host cell. The protein targets used in this study were: SARS-CoV-2 spike glycoprotein, angiotensin-converting enzyme 2, furin and transmembrane serine protease 2. The results showed that the constituents of pomegranate peel extracts, namely punicalagin and punicalin had very promising potential for significant interactions with the selected protein targets and were therefore deemed good candidates for further in vitro and in vivo evaluation.

          Related collections

          Most cited references54

          • Record: found
          • Abstract: found
          • Article: not found

          SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor

          Markus Hoffmann, Hannah Kleine-Weber, Simon Schroeder … (2020)
          Summary The recent emergence of the novel, pathogenic SARS-coronavirus 2 (SARS-CoV-2) in China and its rapid national and international spread pose a global health emergency. Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases. Unravelling which cellular factors are used by SARS-CoV-2 for entry might provide insights into viral transmission and reveal therapeutic targets. Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. A TMPRSS2 inhibitor approved for clinical use blocked entry and might constitute a treatment option. Finally, we show that the sera from convalescent SARS patients cross-neutralized SARS-2-S-driven entry. Our results reveal important commonalities between SARS-CoV-2 and SARS-CoV infection and identify a potential target for antiviral intervention.
          Article 0 comments Cited 9619 times – based on 0 reviews     Review now
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading.

            Oleg Trott, Arthur Olson (2010)
            AutoDock Vina, a new program for molecular docking and virtual screening, is presented. AutoDock Vina achieves an approximately two orders of magnitude speed-up compared with the molecular docking software previously developed in our lab (AutoDock 4), while also significantly improving the accuracy of the binding mode predictions, judging by our tests on the training set used in AutoDock 4 development. Further speed-up is achieved from parallelism, by using multithreading on multicore machines. AutoDock Vina automatically calculates the grid maps and clusters the results in a way transparent to the user. Copyright 2009 Wiley Periodicals, Inc.
            Article 0 comments Cited 4519 times – based on 0 reviews     Review now
              Bookmark
              • Record: found
              • Abstract: found
              • Article: found
              Is Open Access

              Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

              Daniel Wrapp, Nianshuang Wang, Kizzmekia S. Corbett … (2020)
              Structure of the nCoV trimeric spike The World Health Organization has declared the outbreak of a novel coronavirus (2019-nCoV) to be a public health emergency of international concern. The virus binds to host cells through its trimeric spike glycoprotein, making this protein a key target for potential therapies and diagnostics. Wrapp et al. determined a 3.5-angstrom-resolution structure of the 2019-nCoV trimeric spike protein by cryo–electron microscopy. Using biophysical assays, the authors show that this protein binds at least 10 times more tightly than the corresponding spike protein of severe acute respiratory syndrome (SARS)–CoV to their common host cell receptor. They also tested three antibodies known to bind to the SARS-CoV spike protein but did not detect binding to the 2019-nCoV spike protein. These studies provide valuable information to guide the development of medical counter-measures for 2019-nCoV. Science, this issue p. 1260
              Article 0 comments Cited 4149 times – based on 0 reviews     Review now
                Bookmark
                All references

                Author and article information

                Contributors
                Ranko Škrbić:
                ORCID: http://orcid.org/0000-0002-6643-1781
                ranko.skrbic@med.unibl.org
                Journal
                Journal ID (nlm-ta): Mol Cell Biochem
                Journal ID (iso-abbrev): Mol Cell Biochem
                Title: Molecular and Cellular Biochemistry
                Publisher: Springer US (New York )
                ISSN (Print): 0300-8177
                ISSN (Electronic): 1573-4919
                Publication date (Electronic): 16 November 2020
                Pages: 1-15
                Affiliations
                [1 ]GRID grid.35306.33, ISNI 0000 0000 9971 9023, Department of Pharmacognosy, Faculty of Medicine, University of Banja Luka, ; Banja Luka, Bosnia and Herzegovina
                [2 ]GRID grid.35306.33, ISNI 0000 0000 9971 9023, Department of Pharmaceutical chemistry, Faculty of Medicine, University of Banja Luka, ; Banja Luka, Bosnia and Herzegovina
                [3 ]GRID grid.35306.33, ISNI 0000 0000 9971 9023, Department of Pharmacology, Toxicology and Clinical Pharmacology, Faculty of Medicine, , University of Banja Luka, ; Banja Luka, Bosnia and Herzegovina
                [4 ]GRID grid.7149.b, ISNI 0000 0001 2166 9385, Institute of Medical Physiology “Richard Burian”, Faculty of Medicine, , University of Belgrade, ; Belgrade, Serbia
                [5 ]GRID grid.35306.33, ISNI 0000 0000 9971 9023, Faculty of Medicine, , University of Banja Luka, ; Banja Luka, Bosnia and Herzegovina
                [6 ]GRID grid.35306.33, ISNI 0000 0000 9971 9023, Department of Microbiology, Faculty of Medicine, , University of Banja Luka, ; Banja Luka, Bosnia and Herzegovina
                [7 ]GRID grid.508132.d, Department of Hygiene, Public Health Institute of Republic of Srpska, ; Banja Luka, Bosnia and Herzegovina
                [8 ]GRID grid.35306.33, ISNI 0000 0000 9971 9023, Department of Preventive Medicine, Faculty of Medicine, , University of Banja Luka, ; Banja Luka, Bosnia and Herzegovina
                [9 ]Institute for Medicinal Plant Research “Dr Josif Pančić”, Belgrade, Serbia
                Author information
                http://orcid.org/0000-0002-6643-1781
                Article
                Publisher ID: 3981
                DOI: 10.1007/s11010-020-03981-7
                PMC ID: 7668668
                PubMed ID: 33200379
                SO-VID: 7c9f43a7-efbb-424f-9c8d-a6ca51c42363
                Copyright © © Springer Science+Business Media, LLC, part of Springer Nature 2020
                License:

                This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.

                History
                Date received : 28 August 2020
                Date accepted : 6 November 2020
                Categories
                Subject: Article

                ScienceOpen disciplines: Biochemistry
                Keywords: covid-19,sars-cov-2,molecular docking,pomegranate peel extract,punicalagin,punicalin
                Data availability:
                ScienceOpen disciplines: Biochemistry
                Keywords: covid-19, sars-cov-2, molecular docking, pomegranate peel extract, punicalagin, punicalin

                Comments

                Comment on this article

                scite_

                Similar content476

                See all similar

                Cited by21

                See all cited by

                Most referenced authors1,625

                See all reference authors