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.

Studying the interaction of magainin 2 and cecropin a with E. coli bacterial cells using circular dichroism / C. Avitabile, L.D. D’Andrea, A. Romanelli (METHODS IN MOLECULAR BIOLOGY). - In: Antimicrobial Peptides : Methods and Protocols / [a cura di] P.R. Hansen. - Prima edizione. - [s.l] : Humana Press : Springer Nature, 2017. - ISBN 9781493967353. - pp. 247-253 [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

A. Romanelli
Ultimo
2017

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.
Antimicrobial peptides; Circular dichroism; E. coli cells; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Magainins; Protein Binding; Protein Structure, Secondary; Circular Dichroism; Escherichia coli; Molecular Biology; Genetics
Settore CHIM/03 - Chimica Generale e Inorganica
2017
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/580462
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