Abstract：
Helical amphipathic peptides containing cationic and hydrophobic amino acid residues can possess potent antimicrobial activity against both Gram-positive and Gram-negative bacteria. In this study, several amphipathic peptides with enhanced helical structures containing nonproteinogenic amino acids were designed, and the relationships between the antimicrobial activity, hemolytic activity, and cytotoxicity were evaluated. In particular, the effect on the antimicrobial activity and cytotoxicity of the number and position of stapling structures introduced into the sequence was investigated. Peptide stp1 containing α,α-disubstituted amino acids showed potent antimicrobial activity against multidrug-resistant bacteria (MDRP, SP45, and Staphylococcus aureus) without causing appreciable hemolytic activity or cytotoxicity. The cytotoxicity was found to be somewhat correlated to the hydrophobicity of the peptides.
摘要：
含有阳离子和疏水性氨基酸残基的螺旋两亲性肽可具有针对革兰氏阳性和革兰氏阴性细菌两者的有效抗微生物活性。在这项研究中,设计了几种含有非蛋白质氨基酸的增强螺旋结构的两亲性肽，以及抗菌活性之间的关系，溶血活性,和细胞毒性进行评估。特别是,研究了引入序列的钉合结构的数量和位置对抗菌活性和细胞毒性的影响。含α的肽stp1，α-二取代氨基酸对多重耐药细菌显示出有效的抗菌活性(MDRP，SP45和金黄色葡萄球菌），不会引起明显的溶血活性或细胞毒性。发现细胞毒性与肽的疏水性有些相关。
