Polymyxin B and polymyxin B nonapeptide alter cytoplasmic membrane permeability in Escherichia coli.

R A Dixon, I Chopra
Author Information

Abstract

The effects of polymyxin B and polymyxin B nonapeptide (PMBN) on the permeability of the Escherichia coli cytoplasmic membrane were investigated. Both compounds caused loss of free amino acids, uracil and K+ from E. coli. The rates of loss promoted by polymyxin B were one and a half to two-fold greater than those caused by PMBN. Although PMBN mediated loss of low molecular weight substances from E. coli, it was not bactericidal. In contrast, polymyxin B treated E. coli lysed and rapidly lost viability. We suggest that the bactericidal activity of polymyxin B may be related to its previously reported ability to release cytoplasmic proteins from bacteria.

MeSH Term

Amino Acids
Cell Membrane
Cell Membrane Permeability
Escherichia coli
Polymyxin B
Polymyxins
Potassium
Uracil

Chemicals

Amino Acids
Polymyxins
Uracil
polymyxin B nonapeptide
Polymyxin B
Potassium

Word Cloud

Created with Highcharts 10.0.0BpolymyxincoliPMBNcytoplasmiclossEnonapeptidepermeabilityEscherichiamembranecausedbactericidaleffectsinvestigatedcompoundsfreeaminoacidsuracilK+ratespromotedonehalftwo-foldgreaterAlthoughmediatedlowmolecularweightsubstancescontrasttreatedlysedrapidlylostviabilitysuggestactivitymayrelatedpreviouslyreportedabilityreleaseproteinsbacteriaPolymyxinalter

Similar Articles

Cited By