Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    Molecular Docking and 3-D QSAR Studies of Substituted 2,2-Bisaryl-Bicycloheptanes as Human 5-Lipoxygenase-Activating Protein (FLAP) Inhibitors

    Access Status
    Fulltext not available
    Authors
    Ma, X.
    Zhou, L.
    Zuo, Zhili
    Liu, J.
    Yang, M.
    Wang, R.
    Date
    2008
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Ma, Xiang and Zhou, Lu and Zuo, Zhili and Liu, Jian and Yang, Min and Wang, Rong-wei. 2008. Molecular Docking and 3-D QSAR Studies of Substituted 2,2-Bisaryl-Bicycloheptanes as Human 5-Lipoxygenase-Activating Protein (FLAP) Inhibitors. QSAR & Combinatorial Science 27 (9): pp. 1083-1091.
    Source Title
    QSAR & Combinatorial Science
    DOI
    10.1002/qsar.200810053
    ISSN
    1611-020X
    Faculty
    Faculty of Health Sciences
    School of Biomedical Sciences
    URI
    http://hdl.handle.net/20.500.11937/10087
    Collection
    • Curtin Research Publications
    Abstract

    Leukotrienes have been shown to be involved in a variety of diseases such as cardiovascular diseases, cancer, asthma, ulcerative colitis, and rhinitis. 5-Lipoxygenase-Activating Protein (FLAP) was found to be a key enzyme of leukotriene synthesis. Comparative Molecular Field Analysis (CoMFA) and molecular docking studies were carried out on a series of substituted 2,2-bisaryl-bicycloheptanes FLAP inhibitors. The docking results provided a reliable conformational alignment scheme for 3-D QSAR model. Based on the docking conformations, highly predictive CoMFA model was performed with a leave-one-out cross-validated q2 of 0.651. The noncross-validated analysis with four optimum components revealed a conventional r2 value of 0.972, F=175.674, and an estimated standard error of 0.169. The predictive ability of this model was validated by the testing set with a conventional r2 value of 0.920. The analyses may be used to design more potent FLAP inhibitors and predict their activities prior to synthesis.

    Related items

    Showing items related by title, author, creator and subject.

    • Molecular docking of carbohydrate ligands to antibodies: Structural validation against crystal structures
      Agostillo, M.; Jene, C.; Boyle, T.; Ramsland, Paul; Yuriev, E. (2009)
      Cell surface glycoproteins play vital roles in cellular homeostasis and disease. Antibody recognition of glycosylation on different cells and pathogens is critically important for immune surveillance. Conversely, adverse ...
    • Latest developments in molecular docking: 2010-2011 in review
      Yuriev, E.; Ramsland, Paul (2013)
      The aim of docking is to accurately predict the structure of a ligand within the constraints of a receptor binding site and to correctly estimate the strength of binding. We discuss, in detail, methodological developments ...
    • Optimization of protein-protein docking for predicting Fc-protein interactions
      Agostino, Mark; Mancera, R.; Ramsland, P.; Fernández-Recio, J. (2016)
      The antibody crystallizable fragment (Fc) is recognized by effector proteins as part of the immune system. Pathogens produce proteins that bind Fc in order to subvert or evade the immune response. The structural ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.