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Chiroptical Properties of Bilirubin-Serum Albumin Binding Sites

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F13%3A43895072" target="_blank" >RIV/60461373:22340/13:43895072 - isvavai.cz</a>

  • Result on the web

    <a href="http://dx.doi.org/10.1002/chir.22143" target="_blank" >http://dx.doi.org/10.1002/chir.22143</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1002/chir.22143" target="_blank" >10.1002/chir.22143</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Chiroptical Properties of Bilirubin-Serum Albumin Binding Sites

  • Original language description

    Although the interactions between bilirubin and serum albumin are among the most studied serum albumin-ligand interactions, the binding-site location and the participation of bilirubin-serum albumin complexes in pathological and physiological processes are under debate. In this article, we have benefited from the chiral structure of bilirubin and used CD spectroscopy to characterize the structure of bilirubin bound to human and bovine serum albumins. We determined that in a phosphate buffer at pH7.8 there are three binding sites in both human and bovine serum albumins. While the primary binding sites in human and bovine serum albumins bind bilirubin with P- and M-helical conformations, respectively, the secondary binding sites in both albumins bind bilirubin in the P-helical conformation. We have shown that the bonding of bilirubin to the serum albumin matrix is a more favorable process than the self-association of bilirubin under the studied conditions, with a maximum of three bound b

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    FR - Pharmacology and apothecary chemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GAP206%2F11%2F0836" target="_blank" >GAP206/11/0836: Structural Study of Potentially Bioactive Bile Pigment Complexes: Relation to their Protective Function in Organisms</a><br>

  • Continuities

    S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2013

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Chirality

  • ISSN

    0899-0042

  • e-ISSN

  • Volume of the periodical

    25

  • Issue of the periodical within the volume

    4

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    7

  • Pages from-to

    257-263

  • UT code for WoS article

    000316913100007

  • EID of the result in the Scopus database