title: Binding studies of antimicrobial peptides to Escherichia coli cells.
abstract: Understanding the mechanism of action of antimicrobial peptides is pivotal to the design of new and more active peptides. In the last few years it has become clear that the behavior of antimicrobial peptides on membrane model systems does not always translate to cells; therefore the need to develop methods aimed at capturing details of the interactions of peptides with bacterial cells is compelling. In this work we analyzed binding of two peptides, namely temporin B and TB_KKG6A, to Escherichia coli cells and to Escherichia coli LPS. Temporin B is a natural peptide active against Gram positive bacteria but inactive against Gram negative bacteria, TB_KKG6A is an analogue of temporin B showing activity against both Gram positive and Gram negative bacteria. We found that binding to cells occurs only for the active peptide TB_KKG6A; stoichiometry and affinity constant of this peptide toward Escherichia coli cells were determined.
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy.
authors.forename: Concetta
authors.initials: C
authors.lastname: Avitabile
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy.
authors.forename: Luca D
authors.initials: LD
authors.lastname: D'Andrea
authors.affiliation: Istituto di Cristallografia, CNR, Via Amendola 122, 70126 Bari, Italy.
authors.forename: Michele
authors.initials: M
authors.lastname: Saviano
authors.affiliation: Istituto di Genetica e Biofisica "A. Buzzati Traverso", CNR, Via Pietro Castellino 111, 80131 Napoli, Italy.
authors.forename: Michele
authors.initials: M
authors.lastname: Olivieri
authors.affiliation: Istituto di Genetica e Biofisica "A. Buzzati Traverso", CNR, Via Pietro Castellino 111, 80131 Napoli, Italy.
authors.forename: Amelia
authors.initials: A
authors.lastname: Cimmino
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134 Napoli, Italy; Dipartimento di Farmacia, Università di Napoli "Federico II", Via Mezzocannone 16, 80134 Napoli, Italy. Electronic address: alessandra.romanelli@unina.it.
authors.forename: Alessandra
authors.initials: A
authors.lastname: Romanelli
mesh_terms: D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D023181:Antimicrobial Cationic Peptides; D011506:Proteins; C000598077:TB-KKG6A peptide; C104501:temporin
keywords: Antimicrobial; Binding; Cell; Dissociation constant; Peptide; Temporin