Circular Dichroism studies on the interactions of antimicrobial peptides with bacterial cells
Articolo
Data di Pubblicazione:
2014
Citazione:
Circular Dichroism studies on the interactions of antimicrobial peptides with bacterial cells / A. Concetta, D. Luca Domenico, A. Romanelli. - In: SCIENTIFIC REPORTS. - ISSN 2045-2322. - 4:1(2014 Mar 12).
Abstract:
Studying how antimicrobial peptides interact with bacterial cells is pivotal to understand their mechanism of action. In this paper we explored the use of Circular Dichroism to detect the secondary structure of two antimicrobial peptides, magainin 2 and cecropin A, with E. coli bacterial cells. The results of our studies allow us to gain two important information in the context of antimicrobial peptides- bacterial cells interactions: peptides fold mainly due to interaction with LPS, which is the main component of the Gram negative bacteria outer membrane and the time required for the folding on the bacterial cells depends on the peptide analyzed.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Animals; Anti-Bacterial Agents; Antimicrobial Cationic Peptides; Circular Dichroism; Escherichia coli; Lipopolysaccharides; Magainins; Protein Folding; Protein Structure, Secondary; Time Factors; Xenopus Proteins; Xenopus laevis; Multidisciplinary
Elenco autori:
A. Concetta, D. Luca Domenico, A. Romanelli
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