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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
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
Alexander Butlerov Institute of Chemistry, Kazan Federal University.
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2014 (English)In: Journal of Molecular Structure, ISSN 0022-2860, E-ISSN 1872-8014, Vol. 1070, p. 38-42Article in journal (Refereed) Published
Abstract [en]

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 -helical central part and an /310-helical C-terminal region (R.P.R. Nanga et al., JACS, 2009, 131, 17972). 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.

Place, publisher, year, edition, pages
2014. Vol. 1070, p. 38-42
National Category
Physical Chemistry
Research subject
Chemistry of Interfaces
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URN: urn:nbn:se:ltu:diva-14256DOI: 10.1016/j.molstruc.2014.04.019ISI: 000337884900005Scopus ID: 2-s2.0-84901924527Local ID: d9b7aca3-5fef-42b5-913c-ef1901fdb3beOAI: oai:DiVA.org:ltu-14256DiVA, id: diva2:987210
Note
Validerad; 2014; 20140422 (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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