Effect of synthetic antimicrobial peptides on Naegleria fowleri trophozoites.

Supathra Tiewcharoen, Watchara Phurttikul, Jundee Rabablert, Prasert Auewarakul, Sittiruk Roytrakul, Pruksawan Chetanachan, Thassanant Atithep, Virach Junnu
Author Information

Abstract

We evaluated the effect of tritrpticin, lactoferrin, killer decapeptide and scrambled peptide in vitro against Naegleria fowleri trophozoites compared with amphotericin B. Tritrpticin (100 microg/ml) caused apoptosis of N. fowleri trophozoites (2x10(5) cells/ml), while lactoferrin, killer decapeptide and scrambled peptide did not. On Gormori trichrome staining, tritrpticin affected the elasticity of the surface membrane and reduced the size of the nuclei of N. fowleri trophozoites. The ultrastructure surface membrane and food cup formation of the trophozoites were 100% inhibited. These results are consistent with inhibition of the nfa1, Mp2CL5 of the treated trophozoite, which plays a role in food cup formation. Tritrpticin 100 microg/ml was not toxic against SK-N-MC cells. Our findings suggest tritrpticin has activity against the surface membrane and nfa1 and Mp2CL5 of N. fowleri trophozoites and could be developed as a potential therapeutic agent.

MeSH Term

Animals
Anti-Infective Agents
Antibodies, Protozoan
Apoptosis
Cell Membrane
Coculture Techniques
Electrophoresis, Polyacrylamide Gel
Humans
Killer Factors, Yeast
Lactoferrin
Membrane Proteins
Microscopy, Electron, Scanning
Naegleria fowleri
Neuroblastoma
Oligopeptides
Peptide Fragments
Polymerase Chain Reaction
Protozoan Proteins
Staining and Labeling
Trophozoites

Chemicals

Anti-Infective Agents
Antibodies, Protozoan
KP killer peptide
Killer Factors, Yeast
Membrane Proteins
Oligopeptides
Peptide Fragments
Protozoan Proteins
tritrpticin
Lactoferrin

Word Cloud

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