Structural highlights
Publication Abstract from PubMedAurelin 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 alpha-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 alpha-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. Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita.,Shenkarev ZO, Panteleev PV, Balandin SV, Gizatullina AK, Altukhov DA, Finkina EI, Kokryakov VN, Arseniev AS, Ovchinnikova TV Biochem Biophys Res Commun. 2012 Dec 7;429(1-2):63-9. doi:, 10.1016/j.bbrc.2012.10.092. Epub 2012 Nov 5. PMID:23137541[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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