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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 tekniska universitet, Institutionen för samhällsbyggnad och naturresurser, Kemiteknik.ORCID-id: 0000-0002-6810-1882
Luleå tekniska universitet, Institutionen för samhällsbyggnad och naturresurser, Kemiteknik.ORCID-id: 0000-0003-1067-7990
Alexander Butlerov Institute of Chemistry, Kazan Federal University.
Vise andre og tillknytning
2014 (engelsk)Inngår i: Journal of Molecular Structure, ISSN 0022-2860, E-ISSN 1872-8014, Vol. 1070, s. 38-42Artikkel i tidsskrift (Fagfellevurdert) 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.

sted, utgiver, år, opplag, sider
2014. Vol. 1070, s. 38-42
HSV kategori
Forskningsprogram
Gränsytors kemi
Identifikatorer
URN: urn:nbn:se:ltu:diva-14256DOI: 10.1016/j.molstruc.2014.04.019ISI: 000337884900005Scopus ID: 2-s2.0-84901924527Lokal ID: d9b7aca3-5fef-42b5-913c-ef1901fdb3beOAI: oai:DiVA.org:ltu-14256DiVA, id: diva2:987210
Merknad
Validerad; 2014; 20140422 (andbra)Tilgjengelig fra: 2016-09-29 Laget: 2016-09-29 Sist oppdatert: 2018-07-10bibliografisk kontrollert

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