Spatial structure of HIV-enhancing heptapeptide Glu-Ile-Leu-Asn-His-Met-Lys in solution and in the complex with a model biological membrane

I. Z. Rakhmatullin^a, D. S. Blokhin^a, O. V. Aganova^a, A. R. Yulmetov^b, A. V. Filippov^c, A. V. Aganov^b, V. V. Klochkov<sup>b

a</sup> Institute of Physics, Kazan (Volga region) Federal University
^b Institute of Physics, Kazan (Volga region) Federal University
^c Institute of Physics, Kazan (Volga region) Federal University

Abstract: The spatial structure of a synthetic fragment of SEVI – heptapeptide Glu-Ile-Leu-Asn-His-Met-Lys – in solution and in the complex with a model cell membrane surface (a micelle based on sodium dodecyl sulfate) was determined and described by $^1\mathrm H$ NMR spectroscopy and two-dimensional NMR (TOCSY, HSQC-HECADE, NOESY) spectroscopy. The complexation was confirmed by the change in the chemical shifts of the heptapeptide's $^1\mathrm H$ NMR spectra as well as by the signs and values of NOE effects in various media. A comparison of the spatial structure of heptapeptide Glu-Ile-Leu-Asn-His-Met-Lys in water solution and in the complex was made.

Keywords: oligopeptides, micelles, NMR $^1\mathrm H$ spectroscopy, TOCSY, NOESY.

UDC: 541.12.038.2+536.75+536.728

Received: 01.02.2012