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Spatial Structures of PAP(262–270) and PAP(274–284), Two Selected Fragments of PAP(248–286), an Enhancer of HIV Infectivity
Institute of Physics, Kazan (Volga Region) Federal University.
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0002-6810-1882
Luleå University of Technology, Department of Civil, Environmental and Natural Resources Engineering, Chemical Engineering.ORCID iD: 0000-0003-1067-7990
Karlsruhe Institute of Technology.
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2015 (English)In: Applied Magnetic Resonance, ISSN 0937-9347, E-ISSN 1613-7507, Vol. 46, no 7, p. 757-769Article in journal (Refereed) Published
Abstract [en]

Prostatic acid phosphatase (PAP) assembles into amyloid fibrils that facilitate infection by HIV. Its peptide fragments PAP(248–286) and PAP(85–120) also enhance attachment of the virus by viral adhesion to the host cell prior to receptor-specific binding via reducing the electrostatic repulsion between the membranes of the virus and the target cell. The secondary structure of monomeric PAP(248–286) in a biomembrane-mimicking environment can be separated into an N-terminal unordered region, an α-helical central domain, and an α/310-helical C-terminal section (Nanga et al., J. Am. Chem. Soc., 131:17972–17979, 2009). In this work, we used two-dimensional nuclear magnetic resonance (2D NMR) spectroscopy techniques to study spatial structures of isolated central [PAP(262–270)] and C-terminal [PAP(274–284)] fragments of PAP(248–286) in SDS micelle solutions. NMR studies revealed the formation of complexes of both peptides with SDS micelles, with attraction to the micelle membranes occurring mainly through nonpolar and uncharged residues of the peptides. We demonstrate that, when interacting with SDS micelles, PAP(262–270) and PAP(274–284) form α-helical and 310-helical secondary structures, respectively, similar to that found previously for the 39-residue PAP(248–286).

Place, publisher, year, edition, pages
2015. Vol. 46, no 7, p. 757-769
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
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URN: urn:nbn:se:ltu:diva-10670DOI: 10.1007/s00723-015-0669-0ISI: 000356813300005Scopus ID: 2-s2.0-84932196596Local ID: 981f0409-cffc-4ae6-9c67-05d8854deb62OAI: oai:DiVA.org:ltu-10670DiVA, id: diva2:983616
Note
Validerad; 2015; Nivå 2; 20150409 (andbra)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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