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In Silico Identification of Potential Inhibitors of Dengue Mosquito, Aedes Aegypti Chorion Peroxidase

Received: 14 May 2014     Accepted: 10 June 2014     Published: 20 June 2014
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Abstract

The three dimensional structure of Aedes aegypti chorion peroxidase was computed by homology modeling. The ModWeb server provided the most accurate model with QMEAN score of 0.642. The protein model consists of 36.1% alpha-helices and 1% beta-strand. Ligand binding sites in Aedes aegypti chorion peroxidase were identified using SiteComp server. In silico docking of a subset of ZINC natural products database was focused on the predicted binding site. Three ligands were found to be potential inhibitors of Ae. aegypti chorion peroxidase.

Published in Computational Biology and Bioinformatics (Volume 2, Issue 3)
DOI 10.11648/j.cbb.20140203.12
Page(s) 38-42
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2014. Published by Science Publishing Group

Keywords

Homology Modeling, Aedes Aegyti, Chorion Peroxidase, Binding Site, In Silico Screening

References
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Cite This Article
  • APA Style

    Edwin Plata Alcantara. (2014). In Silico Identification of Potential Inhibitors of Dengue Mosquito, Aedes Aegypti Chorion Peroxidase. Computational Biology and Bioinformatics, 2(3), 38-42. https://doi.org/10.11648/j.cbb.20140203.12

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    ACS Style

    Edwin Plata Alcantara. In Silico Identification of Potential Inhibitors of Dengue Mosquito, Aedes Aegypti Chorion Peroxidase. Comput. Biol. Bioinform. 2014, 2(3), 38-42. doi: 10.11648/j.cbb.20140203.12

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    AMA Style

    Edwin Plata Alcantara. In Silico Identification of Potential Inhibitors of Dengue Mosquito, Aedes Aegypti Chorion Peroxidase. Comput Biol Bioinform. 2014;2(3):38-42. doi: 10.11648/j.cbb.20140203.12

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  • @article{10.11648/j.cbb.20140203.12,
      author = {Edwin Plata Alcantara},
      title = {In Silico Identification of Potential Inhibitors of Dengue Mosquito, Aedes Aegypti Chorion Peroxidase},
      journal = {Computational Biology and Bioinformatics},
      volume = {2},
      number = {3},
      pages = {38-42},
      doi = {10.11648/j.cbb.20140203.12},
      url = {https://doi.org/10.11648/j.cbb.20140203.12},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.cbb.20140203.12},
      abstract = {The three dimensional structure of Aedes aegypti chorion peroxidase was computed by homology modeling. The ModWeb server provided the most accurate model with QMEAN score of 0.642. The protein model consists of 36.1% alpha-helices and 1% beta-strand. Ligand binding sites in Aedes aegypti chorion peroxidase were identified using SiteComp server. In silico docking of a subset of ZINC natural products database was focused on the predicted binding site. Three ligands were found to be potential inhibitors of Ae. aegypti chorion peroxidase.},
     year = {2014}
    }
    

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    T1  - In Silico Identification of Potential Inhibitors of Dengue Mosquito, Aedes Aegypti Chorion Peroxidase
    AU  - Edwin Plata Alcantara
    Y1  - 2014/06/20
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    N1  - https://doi.org/10.11648/j.cbb.20140203.12
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    T2  - Computational Biology and Bioinformatics
    JF  - Computational Biology and Bioinformatics
    JO  - Computational Biology and Bioinformatics
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    AB  - The three dimensional structure of Aedes aegypti chorion peroxidase was computed by homology modeling. The ModWeb server provided the most accurate model with QMEAN score of 0.642. The protein model consists of 36.1% alpha-helices and 1% beta-strand. Ligand binding sites in Aedes aegypti chorion peroxidase were identified using SiteComp server. In silico docking of a subset of ZINC natural products database was focused on the predicted binding site. Three ligands were found to be potential inhibitors of Ae. aegypti chorion peroxidase.
    VL  - 2
    IS  - 3
    ER  - 

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Author Information
  • National Institute of Molecular Biology and Biotechnology, University of the Philippines Los Banos, College, Laguna, Philippines

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