• Port-a-Patch

    世界上最小的膜片钳系统
  • Port-a-Patch

    易学易用——教学的理想工具
  • Port-a-Patch

    可记录细胞、细胞器与脂双层
  • Port-a-Patch

    世界上首款平板芯片膜片钳设备
  • Port-a-Patch

    可进行内灌流——更换细胞内液的理想工具

2019 - High-resolution experimental and computational electrophysiology reveals weak β-lactam binding events in the porin PorB

icon pap   Port-a-Patch publication in Nature Scientific Reports (2019)

Authors:
Bartsch A., Llabrés S., Pein F., Kattner C., Schön M., Diehn M., Tanabe M., Munk A., Zachariae U., Steinem C.

Journal:
Nature Scientific Reports (2019) 9: 1264


Abstract:

The permeation of most antibiotics through the outer membrane of Gram-negative bacteria occurs through porin channels. To design drugs with increased activity against Gram-negative bacteria in the face of the antibiotic resistance crisis, the strict constraints on the physicochemical properties of the permeants imposed by these channels must be better understood. Here we show that a combination of high-resolution electrophysiology, new noise-filtering analysis protocols and atomistic biomolecular simulations reveals weak binding events between the beta-lactam antibiotic ampicillin and the porin PorB from the pathogenic bacterium Neisseria meningitidis. In particular, an asymmetry often seen in the electrophysiological characteristics of ligand-bound channels is utilised to characterise the binding site and molecular interactions in detail, based on the principles of electro-osmotic flow through the channel. Our results provide a rationale for the determinants that govern the binding and permeation of zwitterionic antibiotics in anion-selective porin channels.


Download here

返回总览

We use cookies on our website. Some of them are essential for the operation of the site, while others help us to improve this site and the user experience (tracking cookies). You can decide for yourself whether you want to allow cookies or not. Please note that if you reject them, you may not be able to use all the functionalities of the site.