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Interaction between polyamines and bacterial outer membranes as investigated with ion-selective electrodes.

Takashi Katsu1, Hideki Nakagawa, Keiko Yasuda

  • 1Faculty of Pharmaceutical Sciences, Okayama University, Tsushima, Okayama 700-8530, Japan. katsu@pheasant.pharm.okayama-u.ac.jp

Antimicrobial Agents and Chemotherapy
|March 19, 2002
PubMed
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Polyamines with bulky lipophilic groups effectively permeabilized the Escherichia coli outer membrane. This disruption, measured by tetraphenylphosphonium ion uptake, was enhanced by increasing amino groups and lipophilic moieties.

Area of Science:

  • Microbiology
  • Biochemistry
  • Membrane Biophysics

Background:

  • The outer membrane of Gram-negative bacteria like Escherichia coli acts as a barrier.
  • Polyamines are essential molecules involved in various cellular processes.
  • Understanding how molecules interact with and permeabilize the outer membrane is crucial for developing new antimicrobial strategies.

Purpose of the Study:

  • To investigate the interaction of polyamines with the Escherichia coli outer membrane.
  • To determine the structural requirements of polyamines for inducing outer membrane permeabilization.
  • To compare the efficacy of polyamines in permeabilizing the outer membrane with known agents.

Main Methods:

  • Potentiometric measurements using calcium (Ca2+), tetraphenylphosphonium (TPP+), and potassium (K+) electrodes.

Related Experiment Videos

  • Assessing Ca2+ release from the outer membrane.
  • Monitoring TPP+ uptake to evaluate outer membrane permeabilization.
  • Measuring K+ efflux to assess cytoplasmic membrane permeabilization.

    • Main Results:

    • Increasing the number of amino groups in polyamines enhanced Ca2+ release from the outer membrane.
    • Simple polyamines did not cause TPP+ uptake, indicating no significant outer membrane permeabilization.
    • Polyamines with attached lipophilic moieties and multiple amino groups effectively induced TPP+ uptake.
    • 1-naphthylacetylspermine and methoctramine demonstrated significant outer membrane permeabilization, comparable to polymyxin B nonapeptide.

    Conclusions:

    • Both the number of amino groups and the presence of bulky lipophilic moieties are critical for polyamines to permeabilize the E. coli outer membrane.
    • Specific polyamine derivatives show potential as agents to disrupt the outer membrane barrier.
    • These findings contribute to understanding the mechanisms of outer membrane disruption and could inform the design of novel antibacterial agents.