孔蛋白
精胺
化学
生物物理学
离子通道
频道(广播)
生物化学
生物
基因
受体
大肠杆菌
细菌外膜
计算机科学
酶
计算机网络
作者
Stéphanie Vidal,Pierre Brouant,Jacqueline Chevalier,Monique Malléa,Jacques Barbe,Jean‐Marie Pagès
出处
期刊:PubMed
日期:2002-06-21
卷期号:16 (2): 111-6
被引量:1
摘要
Porin channels play a prominent role during fluoroquinolone uptake and spermine strongly alters the diffusion rate of norfloxacine. Consequently the interactions between spermine and bacterial porin were studied by computer simulation. The results indicate that various residues (E62, D 113, E 117,...) closely located in the internal eyelet region of the OmpF channel are potential binding sites. Among them, the D 113 residue, seems to play an important role in the association channel-spermine. This interaction introduces several changes in the internal morphology of the channel which are responsible for the inhibition of antibiotic uptake using the porin route.
科研通智能强力驱动
Strongly Powered by AbleSci AI