• Title of article

    Vesicle — α-amino acid and vesicle–amide interactions: effects of added α-amino acids and amides on gel to liquid–crystal transitions for four aqueous vesicular systems

  • Author/Authors

    Michael J. Blandamer، نويسنده , , Barbara Briggs، نويسنده , , Paul M. Cullis، نويسنده , , Keith D. Irlam، نويسنده , , Jan B.F.N. Engberts، نويسنده , , Lisette Streefland، نويسنده ,

  • Issue Information
    دوهفته نامه با شماره پیاپی سال 2000
  • Pages
    7
  • From page
    173
  • To page
    179
  • Abstract
    Interactions of α-amino acids, glycine (gly), valine (val), leucine (leu) and phenylalanine (phe) and the closely related phenylalaninamide (phea) with cationic vesicles formed by dimethyldioctadecylammonium bromide (DOAB), dihexadecyldimethylammonium bromide (DHAB), with anionic vesicles formed by sodium ditetradecyl phosphate (DTP) and with zwitterionic vesicles formed by dimyristoyl (C14:0) phosphatidylcholine (DMPC) have been probed using differential scanning microcalorimetry (DSC). Gel-to-liquid transitions for DTP, DOAB, DHAB and DMPC vesicular systems are relatively unaffected by added α-amino acids. In contrast added phea markedly changes the recorded scans for DSC for DTP and DMPC vesicular systems indicating that small changes in the structure of added solutes can have dramatic effects on the structures and thermal characteristics of the vesicles in aqueous suspensions. The results indicate, perhaps surprisingly, that α-amino acids are not incorporated into the bilayers whereas phea is incorporated into DTP and DMPC bilayers.
  • Keywords
    Na+/K+-ATPase , Mice , Thermoanalytical techniques
  • Journal title
    Thermochimica Acta
  • Serial Year
    2000
  • Journal title
    Thermochimica Acta
  • Record number

    1194928