Fluorescence energy transfer study of the lipid bilayer interactions with truncated apolipoprotein a-i mutants

Authors

  • M. S. Girych V. N. Karazin Kharkiv National University image/svg+xml Author
  • I. L. Maliyov V. N. Karazin Kharkiv National University image/svg+xml Author
  • M. V. Romanova V. N. Karazin Kharkiv National University image/svg+xml Author
  • G. P. Gorbenko V. N. Karazin Kharkiv National University image/svg+xml Author
  • E. Adachi Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima Author
  • C. Mizuguchi Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima Author
  • J. G. Molotkovsky Institute of Bioorganic Chemistry, Russian Academy of Sciences Author
  • H. Saito Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima Author

Keywords:

Förster resonance energy transfer, lipid bilayer, Thioflavin T, apolipoprotein A-I.

Abstract

Förster resonance energy transfer (FRET) between anthrylvinyl-labeled phosphatidylcholine (AV-PC) as
a donor and Thioflavin T (ThT) as an acceptor has been employed to explore the binding of N-terminal
fragments of wild (A83) and amyloidogenic variants of apolipoprotein A-I (apoA-I) with substitution
mutations G26R, G26R/W@8, G26R/W@50 and G26R/W@72 to the model membranes composed of
phosphatidylcholine (PC). Analysis of the experimental data in terms of 2D FRET model combined with
the partition model revealed that ThT distance from the lipid bilayer center falls in the range 1.7-2.5 nm,
suggesting that the dye is located in the interfacial membrane region, at the level of phospholipid
headgroups, while partition coefficient characterizing ThT distribution between the aqueous and lipid
phases was estimated to be ca. 4×102. Interaction of monomeric apoA-I N-terminal fragments with PC
liposomes resulted in the increase of AV-ThT FRET efficiency, while this parameter displayed
ambiguous behavior upon membrane binding of fibrillar apoA-I mutants. These findings were
rationalized in terms of the existence of discrete lipid-binding sites within the fibril structure. It was
demonstrated that FRET technique can be employed for ascertaining specific modes of fibril-membrane
interactions.

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Author Biographies

  • M. S. Girych, V. N. Karazin Kharkiv National University

    4 Svobody Sq., 61022, Kharkiv, Ukraine

  • I. L. Maliyov, V. N. Karazin Kharkiv National University

    4 Svobody Sq., 61022, Kharkiv, Ukraine

  • M. V. Romanova, V. N. Karazin Kharkiv National University

    4 Svobody Sq., 61022, Kharkiv, Ukraine

  • G. P. Gorbenko, V. N. Karazin Kharkiv National University

    4 Svobody Sq., 61022, Kharkiv, Ukraine

  • E. Adachi, Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima


    1-78-1 Shomachi, Tokushima 770-8505, Japan

  • C. Mizuguchi, Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima

    1-78-1 Shomachi, Tokushima 770-8505, Japan

  • J. G. Molotkovsky, Institute of Bioorganic Chemistry, Russian Academy of Sciences

    Institute of Bioorganic Chemistry, Russian Academy of Sciences

  • H. Saito, Institute of Health Biosciences and Graduate School of Pharmaceutical Sciences, The University of Tokushima

    1-78-1 Shomachi, Tokushima 770-8505, Japan

How to Cite

Fluorescence energy transfer study of the lipid bilayer interactions with truncated apolipoprotein a-i mutants. (2015). Biophysical Bulletin, 1(29). https://periodicals.karazin.ua/biophysvisnyk/article/view/2327

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