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.

译文

Aurelin是从scyphoid水母Aurelia aurita的mezoglea中分离出的40残基阳离子抗菌肽。Aurelin及其 (15)N标记的类似物在大肠杆菌中过表达并纯化。研究了重组肽的抗菌活性,并通过NMR光谱研究了其空间结构。Aurelin代表紧凑的小球,包含一个3(10)-螺旋和两个由三个二硫键交联的 α-螺旋区域。该肽即使在生理盐浓度下也与阴离子脂质 (POPC/DOPG,3:1) 囊泡结合,它不与两性离子 (POPC) 囊泡相互作用,并且通过两个 α 螺旋区域以中等亲和力与DPC胶束表面相互作用。尽管aurelin显示出与海葵的BgK和ShK毒素的结构同源性,但其表面不具有与K ()-通道高亲和力相互作用所需的 “功能性二体”。获得的数据允许将aurelin的适度抗菌特性和膜活性相关联。

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