• DocumentCode
    2387519
  • Title

    Influence of supramolecular architecture upon the molecular mobility of elastin

  • Author

    Samouillan, V. ; Dandurand, J. ; Lacabanne, C. ; Hornebeck, W.

  • Author_Institution
    Lab. de Phys. des Polymeres, Univ. Paul Sabatier, Toulouse, France
  • fYear
    2002
  • fDate
    2002
  • Firstpage
    334
  • Lastpage
    337
  • Abstract
    Mature elastin is a cross-linked polymer responsible for elastic recoil in various connective tissues. The most probable model for the secondary structure seems to be a dynamic blend between a random coil network and an anisotropic model with the alternation of α helices and recurrent or isolated β turns. We compare the chain dynamics of native elastin purified from bovine neck ligament and its insoluble products obtained from enzymatic digestion. The soluble, uncross-linked derivative is also analysed to obtain new information on the influence of network on elastin molecular mobility. TSC and DDS experiments bring to the fore secondary and main modes for elastin and its derivatives. It has been highlighted that elastolysis and cross-linking do not affect the localised motions, but modify in a significant manner more delocalised motions along the polypeptidic chains.
  • Keywords
    intramolecular mechanics; permittivity; proteins; thermally stimulated currents; α-helix; β-turn; DDS; TSC; anisotropic model; bovine neck ligament; connective tissue; cross-linked polymer; dynamic blend; elastic recoil; elastin; elastolysis; enzymatic digestion; molecular mobility; polypeptidic chain dynamics; random coil network; secondary structure; supramolecular architecture; Bovine; Dielectrics; Elasticity; Frequency; Ligaments; Neck; Peptides; Polymers; Proteins; Temperature;
  • fLanguage
    English
  • Publisher
    ieee
  • Conference_Titel
    Electrets, 2002. ISE 11. Proceedings. 11th International Symposium on
  • Print_ISBN
    0-7803-7560-2
  • Type

    conf

  • DOI
    10.1109/ISE.2002.1043011
  • Filename
    1043011