A polyalanine peptide derived from polar fish with anti-infectious activities

Due to the growing concern about antibiotic-resistant microbial infections, increasing support has been given to new drug discovery programs. A promising alternative to counter bacterial infections includes the antimicrobial peptides (AMPs), which have emerged as model molecules for rational design...

Full description

Saved in:
Bibliographic Details
Published in:Scientific reports 2016-02, Vol.6 (1), p.21385-21385, Article 21385
Main Authors: Cardoso, Marlon H, Ribeiro, Suzana M, Nolasco, Diego O, de la Fuente-Núñez, César, Felício, Mário R, Gonçalves, Sónia, Matos, Carolina O, Liao, Luciano M, Santos, Nuno C, Hancock, Robert E W, Franco, Octávio L, Migliolo, Ludovico
Format: Article
Language:English
Subjects:
Animals
Anti-Infective Agents - pharmacology
Antibiotic resistance
Antibiotics
Bacteria
Bacteria - drug effects
Bacterial infections
Bacterial Infections - drug therapy
Cold Climate
Drug discovery
Flounder
Gram-negative bacteria
Humans
Infections
Peptides - pharmacology
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Due to the growing concern about antibiotic-resistant microbial infections, increasing support has been given to new drug discovery programs. A promising alternative to counter bacterial infections includes the antimicrobial peptides (AMPs), which have emerged as model molecules for rational design strategies. Here we focused on the study of Pa-MAP 1.9, a rationally designed AMP derived from the polar fish Pleuronectes americanus. Pa-MAP 1.9 was active against Gram-negative planktonic bacteria and biofilms, without being cytotoxic to mammalian cells. By using AFM, leakage assays, CD spectroscopy and in silico tools, we found that Pa-MAP 1.9 may be acting both on intracellular targets and on the bacterial surface, also being more efficient at interacting with anionic LUVs mimicking Gram-negative bacterial surface, where this peptide adopts α-helical conformations, than cholesterol-enriched LUVs mimicking mammalian cells. Thus, as bacteria present varied physiological features that favor antibiotic-resistance, Pa-MAP 1.9 could be a promising candidate in the development of tools against infections caused by pathogenic bacteria.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep21385