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Ocellatin‐ PT antimicrobial peptides: High‐resolution microscopy studies in antileishmania models and interactions with mimetic membrane systems
Author(s) -
Oliveira Mayara,
GomesAlves Ana Georgina,
Sousa Carla,
Mirta Marani Mariela,
Plácido Alexandra,
Vale Nuno,
DelerueMatos Cristina,
Gameiro Paula,
Kückelhaus Selma A. S.,
Tomas Ana M.,
S. A. Leite José Roberto,
Eaton Peter
Publication year - 2016
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22925
Subject(s) - antimicrobial peptides , membrane , chemistry , antimicrobial , leishmania infantum , leishmania , secretion , cell membrane , biophysics , cell , bacteria , peptide , mechanism of action , biochemistry , microbiology and biotechnology , in vitro , biology , parasite hosting , organic chemistry , world wide web , computer science , genetics
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.