caa a22 4500 605545529 CHVBK 20210128100936.0 cr unu---uuuuu 210128e20150701xx s 000 0 eng 10.1007/s00723-015-0669-0 doi (NATIONALLICENCE)springer-10.1007/s00723-015-0669-0 Spatial Structures of PAP(262-270) and PAP(274-284), Two Selected Fragments of PAP(248-286), an Enhancer of HIV Infectivity [Elektronische Daten] [Dmiriy Blokhin, Andrei Filippov, Oleg Antzutkin, Sergii Afonin, Vladimir Klochkov] 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). Springer-Verlag Wien, 2015 Blokhin Dmiriy Institute of Physics, Kazan (Volga region) Federal University, Kremlevskaya Str., 18, 420008, Kazan, Russia Federation aut Filippov Andrei Institute of Physics, Kazan (Volga region) Federal University, Kremlevskaya Str., 18, 420008, Kazan, Russia Federation aut Antzutkin Oleg Chemistry of Interfaces, Luleå University of Technology, 91187, Luleå, Sweden aut Afonin Sergii Karlsruhe Institute of Technology, 76021, Karlsruhe, Germany aut Klochkov Vladimir Institute of Physics, Kazan (Volga region) Federal University, Kremlevskaya Str., 18, 420008, Kazan, Russia Federation aut Applied Magnetic Resonance Springer Vienna 46/7(2015-07-01), 757-769 0937-9347 46:7<757 2015 46 723 https://doi.org/10.1007/s00723-015-0669-0 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00723-015-0669-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Blokhin Dmiriy Institute of Physics, Kazan (Volga region) Federal University, Kremlevskaya Str., 18, 420008, Kazan, Russia Federation aut NATIONALLICENCE 700 1- Filippov Andrei Institute of Physics, Kazan (Volga region) Federal University, Kremlevskaya Str., 18, 420008, Kazan, Russia Federation aut NATIONALLICENCE 700 1- Antzutkin Oleg Chemistry of Interfaces, Luleå University of Technology, 91187, Luleå, Sweden aut NATIONALLICENCE 700 1- Afonin Sergii Karlsruhe Institute of Technology, 76021, Karlsruhe, Germany aut NATIONALLICENCE 700 1- Klochkov Vladimir Institute of Physics, Kazan (Volga region) Federal University, Kremlevskaya Str., 18, 420008, Kazan, Russia Federation aut NATIONALLICENCE 773 0- Applied Magnetic Resonance Springer Vienna 46/7(2015-07-01), 757-769 0937-9347 46:7<757 2015 46 723