IPEEC - CENPAT   25619
INSTITUTO PATAGONICO PARA EL ESTUDIO DE LOS ECOSISTEMAS CONTINENTALES
Unidad Ejecutora - UE
artículos
Título:
Ocellatin-PT Antimicrobial Peptides: High Resolution Microscopy Studies in Antileishmania Models and Interactions with Mimetic Membrane Systems
Autor/es:
SOUSA CARLA; ´VALE NUNO; KUCKELHAUS SELMA A.S.; EATON PETER; OLIVEIRA MAYARA; MARANI MARIELA M.; DELERUE-MATOS MARÍA C.; TOMAS ANA M.; GOMES-ALVES ANA G.; PLACIDO ALEXANDRA; GAMEIRO PAULA; LEITE JOSÉ R. S. A.
Revista:
BIOPOLYMERS
Editorial:
JOHN WILEY & SONS INC
Referencias:
Lugar: New York; Año: 2016 vol. 105 p. 873 - 886
ISSN:
0006-3525
Resumen:
The mechanisms of action of antimicrobial peptides (AMPs) on parasites are not fully understood. However, in many cases, AMPs kill target cells by disrupting the cell membrane, their effects being related to their affinities to membranes of varying lipid compositions. New ocellatin-PT peptides were recently isolated from the skin secretion of Leptodactylus pustulatus. In this paper we evaluate ocellatin-PT antiparasitic activity against Leishmania infantum. We characterized the peptide?s secondary structures and evaluated their affinity to different lipid systems using SPR. The results demonstrates that all ocellatins-PT have a solvent-dependent alpha helix structure adoption, five peptides present antiparasitic activity (IC50) lower than 15 µM and that PT-1 and PT-8 show considerable changes in the membranes of the parasite body and a higher affinity for leishmania and bacteria lipid membrane models rather than mammalian lipid membranes, demonstrating selectivity towards parasite model membranes for these AMPs.