title: Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita.
abstract: 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.
authors.affiliation: Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, 117997 Moscow, Russia.
authors.forename: Zakhar O
authors.initials: ZO
authors.lastname: Shenkarev
authors.forename: Pavel V
authors.initials: PV
authors.lastname: Panteleev
authors.forename: Sergey V
authors.initials: SV
authors.lastname: Balandin
authors.forename: Albina K
authors.initials: AK
authors.lastname: Gizatullina
authors.forename: Dmitry A
authors.initials: DA
authors.lastname: Altukhov
authors.forename: Ekaterina I
authors.initials: EI
authors.lastname: Finkina
authors.forename: Vladimir N
authors.initials: VN
authors.lastname: Kokryakov
authors.forename: Alexander S
authors.initials: AS
authors.lastname: Arseniev
authors.forename: Tatiana V
authors.initials: TV
authors.lastname: Ovchinnikova
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000096:biosynthesis* / Q000737:chemistry / Q000494:pharmacology; D001419:Bacteria / Q000187:drug effects; D004926:Escherichia coli; D008823:Micelles; D008969:Molecular Sequence Data; D010713:Phosphatidylcholines / Q000737:chemistry; D010715:Phosphatidylglycerols / Q000737:chemistry; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000737:chemistry / Q000494:pharmacology; D037401:Scyphozoa; D012996:Solutions; D014867:Water / Q000737:chemistry
chemical_list: D023181:Antimicrobial Cationic Peptides; D008823:Micelles; D010713:Phosphatidylcholines; D010715:Phosphatidylglycerols; D011994:Recombinant Proteins; D012996:Solutions; C579346:aurelin protein, Aurelia aurita; D014867:Water; C051388:1,2-dioleoyl-sn-glycero-3-phosphoglycerol; C028694:1-palmitoyl-2-oleoylphosphatidylcholine