Fluorescence energy transfer study of the lipid bilayer interactions with truncated apolipoprotein a-i mutants
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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13. Lakowicz J. R. Principles of fluorescence spectroscopy / J. R. Lakowicz. Springer: New York., 2006.
14. Bulychev A. A. Current methods of biophysical studies / A. A. Bulychev, V. N. Verchoturov, B. A. Gulaev. Vyschaya shkola. Moscow., 1998.
15. Fung B.K. Surface density determination in membranes by fluorescence energy transfer / B. K. Fung, L. Stryer // Biochemistry. – 1978. – V. 17. – P. 5241–5248.
16. Effect of cholesterol on bilayer location of the class A peptide Ac-18A-NH2 as revealed by fluorescence resonance energy transfer / G. Gorbenko, T. Handa, H. Saito [et al.] // Eur. Biophys. J. 2003. – V. 32(8). – P. 703–709.
17. Dale R. The orientational freedom of molecular probes. The orientation factor in intramolecular energy transfer / R. Dale, J. Eisinger, W. Blumberg // Biophys. J. – 1979. – V. 26. – P. 161–193.
18. Differential study of phosphatidylcholine and sphingomyelin in human high-density lipoproteins with lipid-specific fluorescent probes / J. Molotkovsky, E. Manevich, E. Gerasimova [et al.] // Eur. J. Biochem. – 1982. – V. 122. – P. 573–579.
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21. Effects of a lipid environment on the fibrillogenic pathway of the N-terminal polypeptide of human apolipoprotein A-I, responsible for in vivo amyloid fibril formation / D. M. Monti, F. Guglielmi, M. Monti [et al.] // European Biophysics Journal. – 2010. – V. 39. – P. 1289–1299.
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Cited
How to Cite
Girych, M. S., Maliyov, I. L., Romanova, M. V., Gorbenko, G. P., Adachi, E., Mizuguchi, C., Molotkovsky, J. G., & Saito, H. (1). Fluorescence energy transfer study of the lipid bilayer interactions with truncated apolipoprotein a-i mutants. Biophysical Bulletin, 1(29). Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/2327
Section
Cell biophysics
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