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The Characteristic Region of Arenicin-1 Involved with a Bacterial Membrane Targeting Mechanism by Jaeyong Cho; Dong Gun Lee is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The antimicrobial peptide arenicin-1 consists of two antiparallel β-sheets linked by a hydrophilic β-turn. To determine the role of a specific region found in a particular β-sheet structure of the peptide for antibacterial activity, two analogs with N-terminal deletions (RW) and substitutions of Arg to Ala in the β-turn region were designed. In the minimum inhibitory concentration (MIC) test, the antibacterial activities of the analogs were reduced for both Gram-positive and Gram-negative bacteria, when compared to arenicin-1. The influence of the decrease in hydrophobicity on the antibacterial activity was confirmed by a hemolytic assay. Through flow cytometric analysis using propidium iodide (PI) and a 1,6-diphenyl-1,3,5-hexatriene (DPH) assay, it was confirmed that the analogs decreased the degree of plasma membrane permeability compared to arenicin-1. In particular, analog 2 showed a lower permeability in Gram-negative bacteria than in Gram-positive bacteria. The results indicate that a reduction in the net charge weakened the electrostatic interactions between the peptides and the negatively charged membranes. In liposomes, which mimic bacterial membranes, due to a reduced bin

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Author

Jaeyong Cho; Dong Gun Lee

Publisher

Elsevier Science; Elsevier ; Elsevier Inc.; Elsevier BV (ISSN 0006-291X)

Published

2011

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)