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A "building block" approach to the new influenza A virus entry inhibitors with reduced cellular toxicities

tetano

Editor, Senior Moderator
Sci Rep. 2016 Mar 8;6:22790. doi: 10.1038/srep22790.
[h=1]A "building block" approach to the new influenza A virus entry inhibitors with reduced cellular toxicities.[/h] Lin D[SUP]1[/SUP], Li F[SUP]1[/SUP], Wu Q[SUP]1[/SUP], Xie X[SUP]1[/SUP], Wu W[SUP]1[/SUP], Wu J[SUP]2[/SUP], Chen Q[SUP]3[/SUP], Liu S[SUP]1[/SUP], He J[SUP]1[/SUP].
[h=3]Author information[/h]

[h=3]Abstract[/h] Influenza A virus (IAV) is a severe worldwide threat to public health and economic development that results in the emergence of drug-resistant or highly virulent strains. Therefore, it is imperative to develop potent anti-IAV drugs with different modes of action to currently available drugs. Herein, we show a new class of antiviral peptides generated by conjugating two known short antiviral peptides: part-1 (named Jp with the sequence of ARLPR) and part-2 (named Hp with the sequence of KKWK). The new peptides were thus created by hybridization of these two domains at C- and N- termini, respectively. The anti-IAV screening results identified that C20-Jp-Hp was the most potent peptide with IC50 value of 0.53 μM against A/Puerto Rico/8/34 (H1N1) strain. Interestingly, these new peptides display lower toxicities toward mammalian cells and higher therapeutic indices than their prototypes. In addition, the mechanism of action of C20-Jp-Hp was extensively investigated.


PMID: 26952867 [PubMed - in process] PMCID: PMC4782136 Free PMC Article
 
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