Idioma:

Interaction of antimicrobial peptide Plantaricin149a and four analogs with lipid bilayers and bacterial membranes

de Souza Lopes, José Luiz ; Hissa, Denise Cavalcante ; Melo, Vânia Maria Maciel ; Beltramini, Leila Maria

Brazilian journal of microbiology, 2013-12, Vol.44 (4), p.1291-1298 [Periódico revisado por pares]

Brazil: Springer Nature B.V

Texto completo disponível

Citações Citado por

Enviar para

Título:
Interaction of antimicrobial peptide Plantaricin149a and four analogs with lipid bilayers and bacterial membranes
Autor: de Souza Lopes, José Luiz ; Hissa, Denise Cavalcante ; Melo, Vânia Maria Maciel ; Beltramini, Leila Maria
Assuntos: Antimicrobial agents ; Antimicrobial Cationic Peptides - genetics ; Antimicrobial Cationic Peptides - metabolism ; Bacteria ; Bacteria - drug effects ; Bacteriocins - genetics ; Bacteriocins - metabolism ; Cell Membrane - drug effects ; Lactobacillus plantarum - metabolism ; Lipid Bilayers - metabolism ; Lipids ; Membranes ; Microbial Sensitivity Tests ; MICROBIOLOGY ; Peptides ; Pseudomonas aeruginosa - drug effects ; Research Paper ; Staphylococcus aureus - drug effects
É parte de: Brazilian journal of microbiology, 2013-12, Vol.44 (4), p.1291-1298
Descrição: The amidated analog of Plantaricin149, an antimicrobial peptide from Lactobacillus plantarum NRIC 149, directly interacts with negatively charged liposomes and bacterial membranes, leading to their lysis. In this study, four Pln149-analogs were synthesized with different hydrophobic groups at their N-terminus with the goal of evaluating the effect of the modifications at this region in the peptide's antimicrobial properties. The interaction of these peptides with membrane models, surface activity, their hemolytic effect on red blood cells, and antibacterial activity against microorganisms were evaluated. The analogs presented similar action of Plantaricin149a; three of them with no hemolytic effect (< 5%) until 0.5 mM, in addition to the induction of a helical element when binding to negative liposomes. The N-terminus difference between the analogs and Plantaricin149a retained the antibacterial effect on S. aureus and P. aeruginosa for all peptides (MIC50 of 19 μM and 155 μM to Plantaricin149a, respectively) but resulted in a different mechanism of action against the microorganisms, that was bactericidal for Plantaricin149a and bacteriostatic for the analogs. This difference was confirmed by a reduction in leakage action for the analogs. The lytic activity of Plantaricin149a is suggested to be a result of the peptide-lipid interactions from the amphipathic helix and the hydrophobic residues at the N-terminus of the antimicrobial peptide.
Editor: Brazil: Springer Nature B.V
Idioma: Inglês;Português

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Anterior Resultado 7 Avançar Ir para próxima página

Realização: Logos de Redes Sociais:

Interaction of antimicrobial peptide Plantaricin149a and four analogs with lipid bilayers and bacterial membranes

de Souza Lopes, José Luiz ; Hissa, Denise Cavalcante ; Melo, Vânia Maria Maciel ; Beltramini, Leila Maria

Brazil: Springer Nature B.V

Buscando em bases de dados remotas. Favor aguardar.