Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita.

Autor: Shenkarev ZO; Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, 117997 Moscow, Russia., Panteleev PV, Balandin SV, Gizatullina AK, Altukhov DA, Finkina EI, Kokryakov VN, Arseniev AS, Ovchinnikova TV
Jazyk: angličtina
Zdroj: Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2012 Dec 07; Vol. 429 (1-2), pp. 63-9. Date of Electronic Publication: 2012 Nov 05.
DOI: 10.1016/j.bbrc.2012.10.092
Abstrakt: Aurelin is a 40-residue cationic antimicrobial peptide isolated from the mezoglea of a scyphoid jellyfish Aurelia aurita. Aurelin and its (15)N-labeled analogue were overexpressed in Escherichia coli and purified. Antimicrobial activity of the recombinant peptide was examined, and its spatial structure was studied by NMR spectroscopy. Aurelin represents a compact globule, enclosing one 3(10)-helix and two α-helical regions cross-linked by three disulfide bonds. The peptide binds to anionic lipid (POPC/DOPG, 3:1) vesicles even at physiological salt concentration, it does not interact with zwitterionic (POPC) vesicles and interacts with the DPC micelle surface with moderate affinity via two α-helical regions. Although aurelin shows structural homology to the BgK and ShK toxins of sea anemones, its surface does not possess the "functional dyad" required for the high-affinity interaction with the K(+)-channels. The obtained data permit to correlate the modest antibacterial properties and membrane activity of aurelin.
(Copyright © 2012 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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