Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita
- Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya str., 16/10, 117997 Moscow (Russian Federation)
- Institute of Experimental Medicine, Russian Academy of Medical Sciences, Academica Pavlova str., 12, 197376 Saint-Petersburg (Russian Federation)
Highlights: Black-Right-Pointing-Pointer Aurelin was overexpressed in Escherichia coli, and its spatial structure was studied by NMR. Black-Right-Pointing-Pointer Aurelin compact structure encloses helical regions cross-linked by three disulfide bonds. Black-Right-Pointing-Pointer Aurelin shows structural homology to the BgK and ShK toxins of sea anemones. Black-Right-Pointing-Pointer Aurelin binds to the anionic lipid vesicles, but does not interact with zwitterionic ones. Black-Right-Pointing-Pointer Aurelin binds to DPC micelle surface with moderate affinity via two helical regions. -- Abstract: Aurelin is a 40-residue cationic antimicrobial peptide isolated from the mezoglea of a scyphoid jellyfish Aurelia aurita. Aurelin and its {sup 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{sub 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{sup +}-channels. The obtained data permit to correlate the modest antibacterial properties and membrane activity of aurelin.
- OSTI ID:
- 22210352
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 429, Issue 1-2; Other Information: Copyright (c) 2012 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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