Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1862, Issue 11, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.bbamem.2020.183443
Keywords
Antimicrobial peptides; Surface interactions; Membrane permeability; Atomic force microscopy
Categories
Funding
- CONICET from Argentina [PIP 11220130100383CO]
- ANPCyT-FONCyT from Argentina [PICT 2016-0478, PICT 2017-2349]
- Universidad Nacional de Santiago del Estero from Argentina [PI-UNSE 23A/250]
- Universidad Nacional de Quilmes (Programa Microbiologia basica y aplicada a Agronomia, Alimentos y Salud) from Argentina
- Fundacao para a Ciencia e a Tecnologia - Ministerio da Ciencia, Tecnologia e Ensino Superior (FCT-MCTES) from Portugal
- CONICET
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Antimicrobial peptides are small molecules that display antimicrobial activity against a wide range of pathogens. In a previous work, by using model membranes we studied P6, a peptide that shows no antimicrobial activity, and P6.2, which exhibits antibacterial activity. In the present work we aimed to unravel the mode of action of these peptides by studying their interaction in vivo with Escherichia coli and Staphylococcus aureus. In this sense, to study the interactions with bacterial cells and their effect on the bacterial surface, zeta potential, spectroscopic, and microscopic methodologies were applied. P6.2 exhibits a higher affinity toward both bacterial envelopes. The ability of both peptides to disrupt afterwards the bacterial membrane was also studied. Both peptides were able to induce bacterial membrane damage, but higher concentrations of P6 were needed to obtain results comparable to those obtained for P6.2. Additionally, P6.2 exhibited faster damage kinetics. Altogether, these data allow postulating, in a physiologic model, that the lower affinity of P6 for bacterial envelope results in a minor final concentration of the peptide in the bacterial membrane unable to trigger the antimicrobial activity. Finally, the fact that the active P6.2 has the same MIC value for the Gram-positive and Gram-negative bacteria tested, but not the same profile in the permeabilization assays, reinforces the question of whether cell wall components act as electrostatic barriers preventing or minimizing membrane-active AMPs lethal action at the membrane level.
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