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Spatial structure of oligopeptide PAP(248-261), the N-terminal fragment of the HIV enhancer prostatic acid phosphatase peptide PAP(248-286), in aqueous and SDS micelle solutions
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Blokhin, Dmitriy S., Filippov, Andrei V., Antzutkin, Oleg N., Karataeva, Farida Kh. and Klochkov, Vladimir V. (2014) Spatial structure of oligopeptide PAP(248-261), the N-terminal fragment of the HIV enhancer prostatic acid phosphatase peptide PAP(248-286), in aqueous and SDS micelle solutions. Journal of Molecular Structure, Volume 1070 . pp. 38-42. doi:10.1016/j.molstruc.2014.04.019 ISSN 0022-2860.
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Official URL: http://dx.doi.org/10.1016/j.molstruc.2014.04.019
Abstract
Prostatic acid phosphatase (PAP) is an enzyme that facilitates infection of cells by HIV. Its peptide fragment PAP(248-286) forms amyloid fibrils known as SEVI, which 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 PAP(248-286) in aqueous and SDS solutions can be divided into an N-terminal disordered region, an α-helical central part and an α/310-helical C-terminal region (Nanga et al., 2009). In this work, we used NMR spectroscopy to study the spatial structure of the isolated N-terminal fragment of PAP(248-286), PAP(248-261) (GIHKQKEKSRLQGG), in aqueous and SDS micelle solutions. Formation of a PAP(248-261)-SDS complex was confirmed by chemical shift alterations in the 1H NMR spectra of the peptide, as well as by the signs and values of Nuclear Overhauser Effect (NOE). In addition, the PAP(248-261) peptide does not form any specified secondary structure in either aqueous or SDS solutions.
Item Type: | Journal Article | ||||||||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Physics | ||||||||||
Journal or Publication Title: | Journal of Molecular Structure | ||||||||||
Publisher: | Elsevier BV | ||||||||||
ISSN: | 0022-2860 | ||||||||||
Official Date: | 24 July 2014 | ||||||||||
Dates: |
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Volume: | Volume 1070 | ||||||||||
Page Range: | pp. 38-42 | ||||||||||
DOI: | 10.1016/j.molstruc.2014.04.019 | ||||||||||
Status: | Peer Reviewed | ||||||||||
Publication Status: | Published | ||||||||||
Access rights to Published version: | Restricted or Subscription Access |
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