Ma Qingquan, Dong Na, Cao Yanping, Shan Anshan
Laboratory of Molecular Nutrition and Immunity, Institute of Animal Nutrition, Northeast Agricultural University, Harbin 150030, China.
Wei Sheng Wu Xue Bao. 2011 Mar;51(3):346-51.
The amphipathic alpha-helical peptide is an important class of antimicrobial peptides. In this study, a 16-residue-long peptide (VGR16) composed of 8 Val residues in the nonpolar face and 5 Arg residues in the polar face was designed based on the helical wheel projection to produce antimicrobial peptide with improved antibacterial activity accompanied by decreased toxicity.
Antimicrobial activity and toxicity against red blood cells and mammalian cells were investigated to evaluate the biological function of the peptide. In addition, bactericidal kinetics was tested.
Antimicrobial assays revealed that the peptide VGR16 showed antimicrobial activity and their MICs against gram-negative and gram-positive bacteria ranged from 16 microg/ml to 64 microg/ml. VGR16 also exhibited rapid bactericidal action. It was surprisingly found that the peptide displayed no hemolytic activity even at a concentration of 256 microg/ml. Cell culture assays indicated that the peptide VGR16 had low cytotoxicity against mammalian cells.
The results showed that the peptide could be a likely candidate for future antimicrobial applications.
两亲性α-螺旋肽是一类重要的抗菌肽。在本研究中，基于螺旋轮投影设计了一种由16个氨基酸残基组成的肽（VGR16），其非极性面含有8个缬氨酸残基，极性面含有5个精氨酸残基，以制备具有改善的抗菌活性且毒性降低的抗菌肽。
研究了该肽对红细胞和哺乳动物细胞的抗菌活性及毒性，以评估其生物学功能。此外，还测试了杀菌动力学。
抗菌试验表明，肽VGR16具有抗菌活性，其对革兰氏阴性菌和革兰氏阳性菌的最低抑菌浓度范围为16微克/毫升至64微克/毫升。VGR16还表现出快速杀菌作用。令人惊讶的是，即使在浓度为256微克/毫升时，该肽也没有溶血活性。细胞培养试验表明，肽VGR16对哺乳动物细胞具有低细胞毒性。
结果表明，该肽可能是未来抗菌应用的一个潜在候选物。
