Journal
JOURNAL OF MOLECULAR STRUCTURE
Volume 1033, Issue -, Pages 59-66Publisher
ELSEVIER
DOI: 10.1016/j.molstruc.2012.08.018
Keywords
Oligopeptides; Amyloid; SEVI
Categories
Funding
- Russian Foundation for Basic Research [12-04-00011-a]
- Ministry of Education and Science of the Russian Federation [02.740.11.0702]
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Prostatic acid phosphatase (PAP) is a protein abundantly present in human seminal fluid. PAP plays important role in fertilization. Its 39-amino-acid fragment, PAP(248-286), is effective in enhancing infectivity of HIV virus. In this work, we determined the spatial structure in aqueous solution of a heptapeptide within the PAP fragment, containing amino acid residues 266-272 (Glu-Ile-Leu-Asn-His-Met-Lys). We also report the structure of the complex formed by this heptapeptide with sodium dodecyl sulfate micelles, a model of a biological membrane, as determined by H-1 NMR spectroscopy and 2D NMR (TOCSY, HSQC-HECADE, NOESY) spectroscopy. Complex formation was confirmed by chemical shift alterations in the H-1 NMR spectra of the heptapeptide, as well as by the signs and values of NOE effects. We also present a comparison of the spatial structure of Glu-Ile-Leu-Asn-His-Met-Lys in water and in complex with sodium dodecyl sulfate. (C) 2012 Elsevier B.V. All rights reserved.
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