A polyalanine peptide derived from polar fish with anti-infectious activities.
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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. |
Year of Publication | 2016
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Journal | Sci Rep
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Volume | 6
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Pages | 21385
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Date Published | 2016 Feb 26
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ISSN | 2045-2322
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DOI | 10.1038/srep21385
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PubMed ID | 26916401
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PubMed Central ID | PMC4768251
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Grant list | R21 AI098701 / AI / NIAID NIH HHS / United States
R21AI098701 / AI / NIAID NIH HHS / United States
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