Studying the Interaction of Magainin 2 and Cecropin A with E. coli Bacterial Cells Using Circular Dichroism

Concetta Avitabile; Luca Domenico D'Andrea; Alessandra Romanelli

doi:10.1007/978-1-4939-6737-7_17

Studying the Interaction of Magainin 2 and Cecropin A with E. coli Bacterial Cells Using Circular Dichroism

Methods Mol Biol. 2017:1548:247-253. doi: 10.1007/978-1-4939-6737-7_17.

Authors

Concetta Avitabile¹, Luca Domenico D'Andrea¹, Alessandra Romanelli^{2

3}

Affiliations

¹ Institute of Biostructure and Bioimaging CNR, via Mezzocannnone 16, 80134, Naples, Italy.
² Institute of Biostructure and Bioimaging CNR, via Mezzocannnone 16, 80134, Naples, Italy. alessandra.romanelli@unina.it.
³ Department of Pharmacy, University of Naples "Federico II", via Mezzocannone 16, Naples, 80134, Italy. alessandra.romanelli@unina.it.

PMID: 28013509
DOI: 10.1007/978-1-4939-6737-7_17

Abstract

The potential of antimicrobial peptides (AMPs) as an effective therapeutic alternative to classic and current antibiotics has encouraged studies to understand how they interact with the bacterial membrane. Here we describe how to detect, by circular dichroism (CD), the secondary structures of two antimicrobial peptides, magainin 2 and cecropin A, in the presence of E. coli bacterial cells.

Keywords: Antimicrobial peptides; Circular dichroism; E. coli cells.

MeSH terms

Anti-Bacterial Agents / chemistry
Anti-Bacterial Agents / pharmacology
Antimicrobial Cationic Peptides / chemistry*
Antimicrobial Cationic Peptides / metabolism
Antimicrobial Cationic Peptides / pharmacology
Circular Dichroism* / methods
Escherichia coli* / drug effects
Escherichia coli* / metabolism
Magainins / chemistry*
Magainins / metabolism
Magainins / pharmacology
Protein Binding
Protein Structure, Secondary

Substances

Anti-Bacterial Agents
Antimicrobial Cationic Peptides
Magainins
cecropin A