Institute of Bioanalytical Chemistry, Faculty of Chemistry & Mineralogy, Universität Leipzig, Deutscher Platz 5, 04103 Leipzig, Germany.
Center for Biotechnology & Biomedicine, Universität Leipzig, Deutscher Platz 5, 04103 Leipzig, Germany.
Future Med Chem. 2016 Jun;8(10):1035-45. doi: 10.4155/fmc-2016-0083. Epub 2016 Jun 10.
Organisms express a set of antimicrobial peptides (AMP) to protect the host against invading microbes by targeting their membranes or intracellular structures. Structurally optimized proline-rich AMPs (PrAMPs) are substantially more efficient in murine infection models than previously assumed from in vitro activities. Thus, we hypothesized that PrAMPs act synergistically with lytic AMPs intrinsically produced in hosts in response to an infection.
METHODS & RESULTS: Synergistic effects between lytic murine cathelicidin-related AMP (CRAMP) and apidaecin- and oncocin-derivatives were studied in chequerboard assays. Evaluation of fractional inhibitory concentration indices revealed synergies against Escherichia coli, Klebsiella pneumoniae, Acinetobacter baumannii and Pseudomonas aeruginosa.
CRAMP synergistically enhances the activity of proline-rich AMPs, which will allow evaluating their therapeutic potential more precisely in vitro.
生物通过靶向其膜或细胞内结构来表达一组抗微生物肽 (AMP) 以保护宿主免受入侵微生物的侵害。结构优化的富含脯氨酸的 AMP(PrAMP)在鼠类感染模型中的效率比以前根据体外活性所假设的要高得多。因此,我们假设 PrAMP 与宿主固有产生的溶菌 AMP 协同作用以响应感染。
在棋盘分析中研究了溶菌鼠源 cathelicidin 相关 AMP(CRAMP)与 apidaecin 和 oncocin 衍生物之间的协同作用。评估部分抑菌浓度指数显示对大肠杆菌、肺炎克雷伯菌、鲍曼不动杆菌和铜绿假单胞菌具有协同作用。
CRAMP 协同增强富含脯氨酸的 AMP 的活性,这将使我们能够更精确地在体外评估它们的治疗潜力。