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

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 inte...

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Bibliographic Details
Published in:Mendeleev communications 2013-11, Vol.23 (6), p.313-315
Main Authors: Filippov, Andrey, Khakimov, Aidar, Afonin, Sergii, Antzutkin, Oleg N.
Format: Article
Language:English
Subjects:
Acid phosphatase
Binding energy
Chemistry of Interfaces
Fragments
Gibbs free energy
Gränsytors kemi
Insertion
Lipids
Liposomes
NMR spectroscopy
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Summary: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.
ISSN:0959-9436
1364-551X
DOI:10.1016/j.mencom.2013.11.002