Macromolecule biosynthesis assay and fluorescence spectroscopy methods to explore antimicrobial peptide mode(s) of action

Bimal Jana*, Kristin Renee Baker, Luca Guardabassi

*Corresponding author for this work
    2 Citations (Scopus)

    Abstract

    Antimicrobial peptides (AMPs) are viable alternatives to the currently available antimicrobials, and numerous studies have investigated their possible use as therapeutic agents for specific clinical applications. AMPs are a diverse class of antimicrobials that often act upon the bacterial cell membrane but may exhibit additional modes of action. Identification of the multiple modes of action requires a comprehensive study at subinhibitory concentrations and careful data analysis since additional modes of action can be eclipsed by AMP action on the cell membrane. Techniques that measure the biosynthesis rate of macromolecules (e.g., DNA, RNA, protein, and cell wall) and the cytoplasmic membrane proton motive force (PMF) energy can help to unravel the diverse modes of action of AMPs. Here, we present an overview of macromolecule biosynthesis rate measurement and fluorescence spectroscopy methods to identify AMP mode(s) of action. Detailed protocols designed to measure inhibition of DNA, RNA, protein, and cell wall synthesis or membrane de-energization are presented and discussed for optimal application of these two techniques as well as to enable accurate interpretation of the experimental findings.

    Original languageEnglish
    Title of host publicationAntimicrobial Peptides : Methods and Protocols
    Number of pages10
    Volume1548
    PublisherHumana Press
    Publication date2017
    Pages181-190
    ISBN (Print)978-1-4939-6735-3
    ISBN (Electronic)978-1-4939-6737-7
    DOIs
    Publication statusPublished - 2017
    SeriesMethods in Molecular Biology
    Volume1548
    ISSN1064-3745

    Keywords

    • Antimicrobial peptide
    • Fluorescence spectroscopy
    • Macromolecule biosynthesis
    • Membrane de-energization/depolarization
    • Mode(s) of action
    • Proton motive force

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