Ocellatin‐PT antimicrobial peptides: High‐resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems

Although the mechanism of action of antimicrobial peptides (AMPs) is not clear, they can interact electrostatically with the cell membranes of microorganisms. New ocellatin‐PT peptides were recently isolated from the skin secretion of Leptodactylus pustulatus. The secondary structure of these AMPs a...

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Bibliographic Details
Published in:Biopolymers 2016-12, Vol.105 (12), p.873-886
Main Authors: Oliveira, Mayara, Gomes‐Alves, Ana Georgina, Sousa, Carla, Mirta Marani, Mariela, Plácido, Alexandra, Vale, Nuno, Delerue‐Matos, Cristina, Gameiro, Paula, Kückelhaus, Selma A. S., Tomas, Ana M., S. A. Leite, José Roberto, Eaton, Peter
Format: Article
Language:English
Subjects:
Antiinfectives and antibacterials
Antimicrobial Cationic Peptides - chemistry
Antimicrobial peptides
Antiprotozoal Agents - chemistry
atomic force microscopy
Bacteria
Leishmania infantum
Leptodactylus pustulatus
lipid membranes
Lipids
Mammals
Membrane Lipids - chemistry
Membranes
Membranes, Artificial
Microorganisms
Peptides
Protein Structure, Secondary
scanning electron microscopy
Surface chemistry
surface plasmon resonance
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Summary:Although the mechanism of action of antimicrobial peptides (AMPs) is not clear, they can interact electrostatically with the cell membranes of microorganisms. New ocellatin‐PT peptides were recently isolated from the skin secretion of Leptodactylus pustulatus. The secondary structure of these AMPs and their effect on Leishmania infantum cells, and on different lipid surface models was characterized in this work. The results showed that all ocellatin‐PT peptides have an α‐helix structure and five of them (PT3, PT4, PT6 to PT8) have leishmanicidal activity; PT1 and PT2 affected the cellular morphology of the parasites and showed greater affinity for leishmania and bacteria‐mimicking lipid membranes than for those of mammals. The results show selectivity of ocellatin‐PTs to the membranes of microorganisms and the applicability of biophysical methods to clarify the interaction of AMPs with cell membranes.
ISSN:0006-3525
1097-0282
DOI:10.1002/bip.22925