tetano
Editor, Senior Moderator
Virology. 2015 Dec 3;488:249-258. doi: 10.1016/j.virol.2015.11.024. [Epub ahead of print]
[h=1]Identification of small molecules acting against H1N1 influenza A virus.[/h] Agamennone M[SUP]1[/SUP], Pietrantoni A[SUP]2[/SUP], Superti F[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza virus represents a serious threat to public health. The lack of effective drugs against flu prompted researchers to identify more promising viral target. In this respect hemagglutinin (HA) can represent an interesting option because of its pivotal role in the infection process. With this aim we collected a small library of commercially available compounds starting from a large database and performing a diversity-based selection to reduce the number of screened compounds avoiding structural redundancy of the library. Selected compounds were tested for their hemagglutination-inhibiting (HI) ability against two different A/H1N1 viral strains (one of which is oseltamivir sensitive), and 17 of them showed the ability to interact with HA. Five drug-like molecules, in particular, were able to impair hemagglutination of both A/H1N1 viral strains under study and to inhibit cytopathic effect and hemolysis at sub-micromolar level.
Copyright ? 2015 Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] Diverse library; Fusion peptide; Hemagglutinin; Hemolysis; Influenza
PMID: 26655243 [PubMed - as supplied by publisher]
[h=1]Identification of small molecules acting against H1N1 influenza A virus.[/h] Agamennone M[SUP]1[/SUP], Pietrantoni A[SUP]2[/SUP], Superti F[SUP]3[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Influenza virus represents a serious threat to public health. The lack of effective drugs against flu prompted researchers to identify more promising viral target. In this respect hemagglutinin (HA) can represent an interesting option because of its pivotal role in the infection process. With this aim we collected a small library of commercially available compounds starting from a large database and performing a diversity-based selection to reduce the number of screened compounds avoiding structural redundancy of the library. Selected compounds were tested for their hemagglutination-inhibiting (HI) ability against two different A/H1N1 viral strains (one of which is oseltamivir sensitive), and 17 of them showed the ability to interact with HA. Five drug-like molecules, in particular, were able to impair hemagglutination of both A/H1N1 viral strains under study and to inhibit cytopathic effect and hemolysis at sub-micromolar level.
Copyright ? 2015 Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] Diverse library; Fusion peptide; Hemagglutinin; Hemolysis; Influenza
PMID: 26655243 [PubMed - as supplied by publisher]