Physicochemical Mechanism for the Lipid Membrane Binding of Polyarginine : The Favorable Enthalpy Change with Structural Transition from Random Coil to α-Helix

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Author(s)

    • TAKECHI Yuki
    • Faculty of Pharmaceutical Sciences, Himeji Dokkyo University
    • MIZUGUCHI Chiharu
    • Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima
    • TANAKA Masafumi
    • Department of Biophysical Chemistry, Kobe Pharmaceutical University
    • OKAMURA Emiko
    • Faculty of Pharmaceutical Sciences, Himeji Dokkyo University
    • SAITO Hiroyuki
    • Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima

Abstract

Lipid membrane binding of polyarginine with different chain length was evaluated. From our findings, it is suggested that the secondary structural change of polyarginine from random coil to α-helix upon lipid binding facilitates insertion into lipid membrane of the polypeptide, leading to the enhanced membrane penetration of polyarginine.

Journal

  • Chemistry Letters

    Chemistry Letters 41(10), 1374-1376, 2012-10-05

    The Chemical Society of Japan

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  • Supporting Information is available electronically on the CSJ-Journal Web site

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Codes

  • NII Article ID (NAID)
    10031120691
  • NII NACSIS-CAT ID (NCID)
    AA00603318
  • Text Lang
    ENG
  • Article Type
    SHO
  • ISSN
    03667022
  • Data Source
    CJP  J-STAGE 
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