A polyalanine peptide derived from polar fish with anti-infectious activities
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Cardoso-2016-Polyalanine peptide.pdf
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Author(s) • • • • • • • • •
Cardoso, Marlon H.
Ribeiro, Suzana M.
Felício, Mário R.
Gonçalves, Sónia
Matos, Carolina O.
Liao, Luciano M.
Santos, Nuno C.
Hancock, Robert E. W.
Franco, Octávio L.
Migliolo, Ludovico
Date Issued
February 2016
Journal
Scientific Reports
Publisher
Nature Publishing Group
Citation
Cardoso, Marlon H.; Ribeiro, Suzana M.; Nolasco, Diego O.; de la Fuente-Núñez, César; Felício, Mário R.; Gonçalves, Sónia; Matos, Carolina O. et al. “A Polyalanine Peptide Derived from Polar Fish with Anti-Infectious Activities.” Scientific Reports 6 (February 26, 2016): 21385.
Version
Final published version
Abstract
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.
MIT Department
Massachusetts Institute of Technology. Research Laboratory of Electronics
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DOI of Published Version
https://doi.org/10.1038/srep21385