Role of arginine and lysine in the antimicrobial mechanism of histone-derived antimicrobial peptides.
Role of arginine and lysine in the antimicrobial mechanism of histone-derived antimicrobial peptides.
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DOI：
10.1016/j.febslet.2015.11.002
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发表时间：
2015-12-21
期刊：
影响因子：
3.5
通讯作者：
Elmore DE
中科院分区：
文献类型：
--
作者：
Cutrona KJ;Kaufman BA;Figueroa DM;Elmore DE
精氨酸或其他胍基团含量的增加通常会促进细胞穿透肽的易位。然而，相对较少的研究考虑了这些官能团对抗菌肽活性的作用。这项研究比较了三种组蛋白衍生的抗菌肽（buforin II、DesHDAP1 和 parasin）与仅含有赖氨酸或精氨酸阳离子残基的变体的活性。这些肽通过不同的机制发挥作用，因为寄生虫会导致膜透化，而蟾蜍素 II 和 DesHDAP1 则会转移到细菌中。对于所有肽，抗菌活性随着精氨酸含量的增加而增加。较高的精氨酸含量增加了parasin 的透化作用，同时改善了buforin II 和DesHDAP1 的易位。这些观察结果让我们深入了解精氨酸和赖氨酸在这些抗菌肽中的相对重要性。
Translocation of cell-penetrating peptides is often promoted by increased content of arginine or other guanidinum groups. However, relatively little research has considered the role of these functional groups on antimicrobial peptide activity. This study compared the activity of three histone-derived antimicrobial peptides—buforin II, DesHDAP1, and parasin— with variants that contain only lysine or arginine cationic residues. These peptides operate via different mechanisms as parasin causes membrane permeabilization while buforin II and DesHDAP1 translocate into bacteria. For all peptides, antibacterial activity increased with increased arginine content. Higher arginine content increased permeabilization for parasin while it improved translocation for buforin II and DesHDAP1. These observations provide insight into the relative importance of arginine and lysine in these antimicrobial peptides.