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JOURNALS // Mendeleev Communications // Archive

Mendeleev Commun., 2013 Volume 23, Issue 6, Pages 313–315 (Mi mendc2697)

This article is cited in 6 papers

Communications

Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy

A. V. Filippovab, A. M. Khakimova, S. Afoninc, O. N. Antzutkinbd

a Institute of Physics, Kazan Federal University, Kazan, Russian Federation
b Chemistry of Interfaces, Luleå University of Technology, Luleå, Sweden
c Karlsruhe Institute of Technology, Karlsruhe, Germany
d Department of Physics, Warwick University, Coventry, U.K.

Abstract: The effects of five fragments of prostatic acid phosphatase on dimyristoylphosphatidylcholine lipid multi-lamellar liposomes were studied by 2H and 31P NMR spectroscopy and those on planar supported multi-bilayers of the same lipid, by 1H and 31P NMR spectro-scopy. It was found that hydrophobic interaction is a dominated factor of the peptide–membrane binding, while the short α-helical fragments PAP(262-270) and PAP(262-272) strongly interact with the membrane at the interface, generally following to the Gibbs free energy of water-to-interface insertion.

Language: English

DOI: 10.1016/j.mencom.2013.11.002



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