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Mendeleev Communications, 2013, Volume 23, Issue 6, Pages 313–315
DOI: https://doi.org/10.1016/j.mencom.2013.11.002
(Mi mendc2697)
 

This article is cited in 6 scientific papers (total 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.
Full-text PDF (676 kB) Citations (6)
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.
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Document Type: Article
Language: English


Citation: A. V. Filippov, A. M. Khakimov, S. Afonin, O. N. Antzutkin, “Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy”, Mendeleev Commun., 23:6 (2013), 313–315
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