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Outer membrane penetration by (2,3)-methylenepenams.

J S Chapman¹, N H Georgopapadakou

¹Roche Research Center, Nutley, New Jersey 07110.

Antimicrobial Agents and Chemotherapy

|December 1, 1987

Summary

The conformation of penicillin G analogs impacts their entry into Escherichia coli. Open-form analogs and sterically restricted versions showed faster outer membrane penetration than standard penicillin G.

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Area of Science:

Microbiology
Biochemistry
Molecular Biology

Background:

The outer membrane of Gram-negative bacteria, such as Escherichia coli, presents a significant barrier to antibiotic entry.
Porins are protein channels in the outer membrane that facilitate the passage of small molecules, including some antibiotics.
Understanding the factors that influence antibiotic penetration is crucial for developing more effective antimicrobial strategies.

Purpose of the Study:

To investigate how the conformational state of penicillin G analogs affects their penetration through the Escherichia coli outer membrane.
To compare the penetration rates of two sterically restricted penicillin G analogs with different conformations to that of native penicillin G.

Main Methods:

Utilized sterically restricted analogs of penicillin G with distinct conformational properties.
Quantified the penetration rates of these analogs across the Escherichia coli outer membrane.
Compared the penetration efficiency of the analogs with the parent compound, penicillin G.

Main Results:

Both sterically restricted penicillin G analogs demonstrated faster penetration of the Escherichia coli outer membrane compared to native penicillin G.
The analog mimicking an "open" conformation of penicillin G penetrated more rapidly than the analog mimicking a "closed" conformation.
Penetration rates were influenced by the conformational state of the beta-lactam nucleus.

Conclusions:

The conformational flexibility of the beta-lactam nucleus is a key factor influencing the penetration of penicillin G analogs via porin-mediated pathways.
Modifying the conformation of antibiotics may represent a viable strategy to enhance their efficacy against Gram-negative bacteria.
These findings contribute to the understanding of antibiotic-outer membrane interactions and inform the design of novel antibacterial agents.

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