tetano
Editor, Senior Moderator
Angew Chem Int Ed Engl. 2017 Apr 26. doi: 10.1002/anie.201702005. [Epub ahead of print]
[h=1]Multivalent Peptide-Nanoparticle Conjugates for Influenza-Virus Inhibition.[/h] Lauster D[SUP]1[/SUP], Glanz M[SUP]2,[/SUP][SUP]3[/SUP], Bardua M[SUP]4[/SUP], Ludwig K[SUP]5[/SUP], Hellmund M[SUP]6[/SUP], Hoffmann U[SUP]4[/SUP], Hamann A[SUP]4[/SUP], B?ttcher C[SUP]5[/SUP], Haag R[SUP]6[/SUP], Hackenberger CPR[SUP]2,[/SUP][SUP]3[/SUP], Herrmann A[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] To inhibit binding of the influenza A virus to the host cell glycocalyx, we generate multivalent peptide-polymer nanoparticles binding with nanomolar affinity to the virus via its spike protein hemagglutinin. The chosen dendritic polyglycerol scaffolds are highly biocompatible and well suited for a multivalent presentation. We could demonstrate in vitro that by increasing the size of the polymer scaffold and adjusting the peptide density, viral infection is drastically reduced. Such a peptide-polymer conjugate qualified also in an in vivo infection scenario. With this study we introduce the first non-carbohydrate-based, covalently linked, multivalent virus inhibitor in the nano- to picomolar range by ensuring low peptide-ligand density on a larger dendritic scaffold.
? 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
[h=4]KEYWORDS:[/h] antiviral agents; in vivo studies; influenza virus; multivalency; peptides
PMID: 28444849 DOI: 10.1002/anie.201702005
[h=1]Multivalent Peptide-Nanoparticle Conjugates for Influenza-Virus Inhibition.[/h] Lauster D[SUP]1[/SUP], Glanz M[SUP]2,[/SUP][SUP]3[/SUP], Bardua M[SUP]4[/SUP], Ludwig K[SUP]5[/SUP], Hellmund M[SUP]6[/SUP], Hoffmann U[SUP]4[/SUP], Hamann A[SUP]4[/SUP], B?ttcher C[SUP]5[/SUP], Haag R[SUP]6[/SUP], Hackenberger CPR[SUP]2,[/SUP][SUP]3[/SUP], Herrmann A[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] To inhibit binding of the influenza A virus to the host cell glycocalyx, we generate multivalent peptide-polymer nanoparticles binding with nanomolar affinity to the virus via its spike protein hemagglutinin. The chosen dendritic polyglycerol scaffolds are highly biocompatible and well suited for a multivalent presentation. We could demonstrate in vitro that by increasing the size of the polymer scaffold and adjusting the peptide density, viral infection is drastically reduced. Such a peptide-polymer conjugate qualified also in an in vivo infection scenario. With this study we introduce the first non-carbohydrate-based, covalently linked, multivalent virus inhibitor in the nano- to picomolar range by ensuring low peptide-ligand density on a larger dendritic scaffold.
? 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
[h=4]KEYWORDS:[/h] antiviral agents; in vivo studies; influenza virus; multivalency; peptides
PMID: 28444849 DOI: 10.1002/anie.201702005