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Interaction of prostatic acid phosphatase fragments with a lipid bilayer as studied by NMR spectroscopy
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0002-6810-1882
Kazan (Volga Region) Federal University, Kazan.
Karlsruhe Institute of Technology.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Sustainable Process Engineering.ORCID iD: 0000-0003-1067-7990
2013 (English)In: Mendeleev communications (Print), ISSN 0959-9436, E-ISSN 1364-551X, Vol. 23, no 6, p. 313-315Article in journal (Refereed) Published
Abstract [en]

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

Place, publisher, year, edition, pages
2013. Vol. 23, no 6, p. 313-315
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
Identifiers
URN: urn:nbn:se:ltu:diva-9948DOI: 10.1016/j.mencom.2013.11.002ISI: 000328716400002Scopus ID: 2-s2.0-84888395753Local ID: 8aa93b62-501c-4b68-88b3-887b874913b0OAI: oai:DiVA.org:ltu-9948DiVA, id: diva2:982887
Note
Validerad; 2013; 20131107 (andfil)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2018-07-10Bibliographically approved

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Filippov, AndreiAntzutkin, Oleg

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