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

    Stereoselective Binding of Human Serum Albumin

    Access Status
    Fulltext not available
    Authors
    Chuang, Victor
    Otagiri, M.
    Date
    2006
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Chuang, Victor Tuan Giam and Otagiri, Masaki. 2006. Stereoselective Binding of Human Serum Albumin. Chirality. 18 (3): pp. 159-166.
    Source Title
    Chirality
    DOI
    10.1002/chir.20237
    ISSN
    08990042
    School
    School of Pharmacy
    URI
    http://hdl.handle.net/20.500.11937/48357
    Collection
    • Curtin Research Publications
    Abstract

    Stereoselectivity in binding can have a significant effect on the drug disposition such as first-pass metabolism, metabolic clearance, renal clearance, and protein and tissue binding. Human serum albumin (HSA) is able to stereoselectively bind a great number of various endogenous and exogenous compounds. Various experimental data suggested that the two major drug-binding cavities, namely, site I and site II, do not seem to be the stereoselective binding sites of HSA. Stereoselective binding of HSA under disease conditions such as renal and hepatic diseases was found to be enhanced. In addition, site-to-site displacement of a site II-specific drug by another site II-specific drug was found to be stereoselective, too. Endogenous compounds such as long-chain fatty acids and uremic toxins are likely to cause combined direct and cascade effects that contribute to the preferential binding of a particular drug enantiomer. Taking together the findings of other studies, it is highly possible that the stereoselective binding site exists at the interface of the subdomains.

    Related items

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

    • Molecular modelling of the interactions of complex carbohydrates with proteins
      Gandhi, Neha Sureshchandra (2011)
      Glycosaminoglycans (GAGs) are ubiquitous complex carbohydrate molecules present on the cell surfaces and in extracellular matrices (ECM) of vertebrate and invertebrate tissues. The interactions of sulphated GAGs such as ...
    • Long chain fatty acids alter the interactive binding of ligands to the two principal drug binding sites of human serum albumin
      Yamasaki, K.; Hyodo, S.; Taguchi, K.; Nishi, K.; Yamaotsu, N.; Hirono, S.; Chuang, Victor; Seo, H.; Maruyama, T.; Otagiri, M. (2017)
      A wide variety of drugs bind to human serum albumin (HSA) at its two principal sites, namely site I and site II. A number of reports indicate that drug binding to these two binding sites are not completely independent, ...
    • Albumin-drug interaction and its clinical implication
      Yamasaki, K.; Maruyama, T.; Chuang, Victor; Otagiri, M. (2013)
      Background: Human serum albumin acts as a reservoir and transport protein for endogenous (e.g. fatty acids or bilirubin) and exogenous compounds (e.g. drugs or nutrients) in the blood. The binding of a drug to albumin is ...
    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.