tetano
Editor, Senior Moderator
Chem Biol Drug Des. 2015 Jan 8. doi: 10.1111/cbdd.12511. [Epub ahead of print]
[h=1]Antimicrobial peptides derived from fusion peptides of influenza A viruses, a promising approach to designing potent antimicrobial agents.[/h] Wang J[SUP]1[/SUP], Zhong W, Lin D, Xia F, Wu W, Zhang H, Lin L, Liu S, He J.
[h=3]Author information[/h]
[h=3]Abstract[/h] The emergence and dissemination of antibiotic-resistant bacterial pathogens have spurred the urgent need to develop novel antimicrobial agents with different mode of action. In this respect, we turned several fusogenic peptides (FPs) derived from the hemaglutinin glycoproteins (HAs) of IAV into potent antibacterials by replacing the negatively or neutrally charged residues of FPs with positively charged lysines. Their antibacterial activities were evaluated by testing the MICs against a panel of bacterial strains including S. aureus, S. mutans, P. aerugenosa and E. coli. The results showed that peptides HA-FP-1, HA-FP-2-1 and HA-FP-3-1 were effective against both gram positive and gram negative bacteria with MICs ranging from 1.9 to 16.0 μM, while the toxicities toward mammalian cells were low. In addition, the mode of action and the secondary structure of these peptides were also discussed. These data not only provide several potent peptides displaying promising potential in development as broad antimicrobial agents, but also present a useful strategy in designing new antimicrobial agents. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
[h=4]KEYWORDS:[/h] antimicrobial peptides ; fusion peptides; influenza A viruses
PMID: 25581878 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25581878
[h=1]Antimicrobial peptides derived from fusion peptides of influenza A viruses, a promising approach to designing potent antimicrobial agents.[/h] Wang J[SUP]1[/SUP], Zhong W, Lin D, Xia F, Wu W, Zhang H, Lin L, Liu S, He J.
[h=3]Author information[/h]
[h=3]Abstract[/h] The emergence and dissemination of antibiotic-resistant bacterial pathogens have spurred the urgent need to develop novel antimicrobial agents with different mode of action. In this respect, we turned several fusogenic peptides (FPs) derived from the hemaglutinin glycoproteins (HAs) of IAV into potent antibacterials by replacing the negatively or neutrally charged residues of FPs with positively charged lysines. Their antibacterial activities were evaluated by testing the MICs against a panel of bacterial strains including S. aureus, S. mutans, P. aerugenosa and E. coli. The results showed that peptides HA-FP-1, HA-FP-2-1 and HA-FP-3-1 were effective against both gram positive and gram negative bacteria with MICs ranging from 1.9 to 16.0 μM, while the toxicities toward mammalian cells were low. In addition, the mode of action and the secondary structure of these peptides were also discussed. These data not only provide several potent peptides displaying promising potential in development as broad antimicrobial agents, but also present a useful strategy in designing new antimicrobial agents. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
[h=4]KEYWORDS:[/h] antimicrobial peptides ; fusion peptides; influenza A viruses
PMID: 25581878 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25581878