Studies on the Antibacterial Activity and Mechanism of Antimicrobial Peptides Against Drug-Resistant Bacteria

被引:25
|
作者
Luo, Xiaofang [1 ]
Liu, Yanjun [2 ]
Qin, Zuodong [1 ]
Jin, Zhiyuan [1 ]
Xu, Liting [1 ]
Liu, Yang [1 ]
Cao, Linyan [1 ]
He, Fulin [1 ]
Gu, Xiaohong [2 ]
Ouyang, Xiaoping [1 ]
机构
[1] Hunan Univ Sci & Engn, Coll Chem & Bioengn, Key Lab Comprehens Utilizat Advantage Plants Reso, Yongzhou 425000, Hunan, Peoples R China
[2] Cent Hosp Yongzhou, Yongzhou 425000, Hunan, Peoples R China
基金
中国国家自然科学基金;
关键词
Antimicrobial Peptides; Multidrug Resistance; Mechanism; Klebsiella pneumoniae; Acinetobacter baumannii; IN-VITRO PHARMACODYNAMICS; ACINETOBACTER-BAUMANNII; SILVER NANOPARTICLES; KLEBSIELLA-PNEUMONIAE; RISK-FACTORS; POLYMYXIN-B; TIGECYCLINE; INFECTIONS; PROPERTY; STRAINS;
D O I
10.1166/jbn.2018.2528
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
Antibiotic resistance is a growing threat to human health. More than anything else, multidrug-resistant gram-negative bacteria pose the biggest challenge to healthcare, which is predominantly due to the lack of effective therapeutic options. In the present study, we investigated the activities of peptides HX-12A, HX-12B and HX-12C against MDRAB and MDRKP isolates in vitro. Those three peptides displayed high antibacterial activities and rapid bactericidal effects against MDRAB and MDRKP isolates. Additionally, the peptides retained their activity even being present in pH 6.8 and 8.0, salt (NaCl 100 mM, CaCl2 1 mM, MgCl2 1 mM) or human serum (5%), especially peptide HX-12C. Moreover, the killing kinetics and transmission electron microscopy results suggested that the possible sterilization mechanism of peptides is to destroy the cell membrane, which makes it more difficult for bacteria to develop resistance. Thus, these three peptides may be developed into new antimicrobial agents.
引用
收藏
页码:601 / 608
页数:8
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