• DocumentCode
    2091589
  • Title

    Assay for Affinity of Proteins onto Model Biomembrane

  • Author

    Jiang, Jing ; Wang, Shanshan ; Ma, Peixiang ; Qu, Feng ; Luo, Aiqin ; Deng, Yulin

  • Author_Institution
    Beijing Inst. of Technol., Beijing
  • fYear
    2007
  • fDate
    23-27 May 2007
  • Firstpage
    1676
  • Lastpage
    1680
  • Abstract
    In this paper, immobilized artificial membrane (IAM) was selected as the model biomembrane, and packed into capillary column as stationary phase of liquid chromatography to screen the proteins having strong interaction with biomembrane rapidly. The affinity between IAM and ten common proteins (pepsin, bovine serum albumin, casein, transferring, myosin, insulin, hemoglobin, cytochrome C, trypsin, lysozyme), whose pI ranged from 2.0-11.5, were analyzed in different pH mobile phase including acidic, neutral and alkaline buffer. The optimized condition was obtained for the affinity of IAM and proteins. The proteins having strong affinity with IAM were screened out under each pH mobile phase. It can provide the experimental foundation for proteins to be immobilized onto biomembrane to study the membrane related interaction, separation, protein bioactivity, and drug screening and so on.
  • Keywords
    biomembranes; molecular biophysics; proteins; IAM; biomembrane protein affinity; bovine serum albumin; casein; cytochrome C; hemoglobin; immobilized artificial membrane; immobilized proteins; insulin; liquid chromatography; lysozyme; membrane related drug screening; membrane related interaction; membrane related protein bioactivity; membrane related separation; myosin; pepsin; transferring; trypsin; Biological materials; Biological system modeling; Biomembranes; Bovine; Cells (biology); Drugs; Insulin; Lipidomics; Proteins; Silicon compounds;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Complex Medical Engineering, 2007. CME 2007. IEEE/ICME International Conference on
  • Conference_Location
    Beijing
  • Print_ISBN
    978-1-4244-1077-4
  • Electronic_ISBN
    978-1-4244-1078-1
  • Type

    conf

  • DOI
    10.1109/ICCME.2007.4382032
  • Filename
    4382032