title: Circular Dichroism studies on the interactions of antimicrobial peptides with bacterial cells.
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.
authors.affiliation: Diagnostica e Farmaceutica Molecolari Scarl, via Mezzocannone 16, 80134 Napoli.
authors.forename: Concetta
authors.initials: C
authors.lastname: Avitabile
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 16, 80134 Napoli.
authors.forename: Luca Domenico
authors.initials: LD
authors.lastname: D'Andrea
authors.affiliation: Dipartimento di Farmacia, Università di Napoli "Federico II", via Mezzocannone 16, 80134 Napoli.
authors.forename: Alessandra
authors.initials: A
authors.lastname: Romanelli
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry*; D002942:Circular Dichroism; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D008070:Lipopolysaccharides / Q000737:chemistry; D054806:Magainins / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013997:Time Factors; D029867:Xenopus Proteins / Q000737:chemistry*; D014982:Xenopus laevis / Q000378:metabolism
chemical_list: D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D008070:Lipopolysaccharides; D054806:Magainins; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus; C031161:cecropin A