抗菌剂
抗菌肽
肽
两亲性
抗生素耐药性
残留物(化学)
抗生素
化学
先天免疫系统
微生物学
氨基酸
生物化学
生物
有机化学
受体
聚合物
共聚物
作者
Ping‐Chien Lee,Chih‐Ching Yen,Chia-Min Lin,Feng‐Di T. Lung
摘要
Antibiotic‐resistant bacterial infections are becoming a serious health issue and will cause 10 million deaths per year by 2050. As a result, the development of new antimicrobial agents is urgently needed. Antimicrobial peptides (AMPs) are found in the innate immune systems of various organisms to effectively fend off invading pathogens. In this study, we designed a series of AMPs (THL‐2‐1 to THL‐2‐9) with centrosymmetric and amphipathic properties, through substituting different amino acids on the hydrophobic side and at the centrosymmetric position to improve their antimicrobial activity. The results showed that leucine as a residue on the hydrophobic side of the peptide could enhance its antimicrobial activity and that glutamic acid as a centrosymmetric residue could increase the salt resistance of the peptide. Thus, the THL‐2‐3 peptide (KRLLRELKRLL‐NH 2 ) showed the greatest antimicrobial activity (MIC 90 of 16 μM) against Gram‐negative bacteria and had the highest salt resistance and cell selectivity among all the designed peptides. In summary, the results of this study provide useful references for the design of AMPs to enhance antimicrobial activity.
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