AMBROGGIO ERNESTO
Artículos
Título:
Differential activity of lytic α-helical peptides on lactobacilli and lactobacilli-derived liposomes
Autor/es:
SZYMANOWSKI, F.; BALATTI, G.E.; AMBROGGIO, E.; HUGO, A.A.; MARTINI, M.F.; FIDELIO, G.D.; GÓMEZ-ZAVAGLIA, A.; PICKHOLZ, M.; PÉREZ, P.F.
Revista:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Año: 2019 vol. 1861 p. 1069 - 1069
ISSN:
0005-2736
Resumen:
ukaryotic antimicrobial peptides (AMPs) interact with plasma membrane of bacteria, fungi and eukaryotic parasites. Noteworthy, Lactobacillus delbrueckii subsp. lactis (CIDCA 133) and L. delbrueckii subsp. bulgaricus (CIDCA 331) show different susceptibility to human beta-defensins (β-sheet peptides). In the present work we extended the study to α-helical peptides from anuran amphibian (Aurein 1.2, Citropin 1.1 and Maculatin 1.1). We studied the effect on whole bacteria and liposomes formulated with bacterial lipids through growth kinetics, flow cytometry, leakage of liposome content and studies of peptide insertion in lipid monolayers. Growth of strain CIDCA 331 was dramatically inhibited in the presence of all three peptides and minimal inhibitory concentrations were lower than those for strain CIDCA 133. Flow cytometry revealed that AMPs lead to the permeabilization of bacteria. In addition, CIDCA 331-derived liposomes showed high susceptibility, leading to content leakage