University of Naples Federico II, School of Biotechnological Sciences, Department of Biological Sciences, Naples, Italy.
J Pept Sci. 2013 Apr;19(4):240-5. doi: 10.1002/psc.2479. Epub 2013 Feb 19.
Cysteine-containing antimicrobial peptides of diverse phylogeny share a common structural signature, the γ core, characterized by a strong polarization of charges in two antiparallel β sheets. In this work, we analyzed peptides derived from the tomato defensin SolyC07g007760 corresponding to the protein γ core and demonstrated that cyclization of the peptides, which results in segregation of positive charges to the turn region, produces peptides very active against Gram negative bacteria, such as Salmonella enterica and Helicobacter pylori. Interestingly, these peptides show very low hemolytic activity and thus represent a scaffold for the design of new antimicrobial peptides.
具有不同系统发育的含半胱氨酸的抗菌肽具有共同的结构特征，即 γ 核心，其特征在于两个反平行 β 片层中的电荷强烈极化。在这项工作中，我们分析了来自番茄防御素 SolyC07g007760 的衍生肽，这些肽对应于蛋白质 γ 核心，并证明肽的环化导致正电荷向环区分离，产生了对革兰氏阴性菌（如肠炎沙门氏菌和幽门螺杆菌）非常有效的肽。有趣的是，这些肽的溶血活性非常低，因此它们代表了设计新型抗菌肽的支架。
