tetano
Editor, Senior Moderator
Carbohydr Res. 2016 Sep 28;435:68-75. doi: 10.1016/j.carres.2016.09.017. [Epub ahead of print]
[h=1]Multivalent S-sialoside protein conjugates block influenza hemagglutinin and neuraminidase.[/h] Yang Y[SUP]1[/SUP], Liu HP[SUP]2[/SUP], Yu Q[SUP]2[/SUP], Yang MB[SUP]2[/SUP], Wang DM[SUP]2[/SUP], Jia TW[SUP]2[/SUP], He HJ[SUP]2[/SUP], He Y[SUP]3[/SUP], Xiao HX[SUP]4[/SUP], Iyer SS[SUP]5[/SUP], Fan ZC[SUP]6[/SUP], Meng X[SUP]7[/SUP], Yu P[SUP]8[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] A new class of S-sialoside Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) conjugates were prepared to enhance the binding affinity to hemagglutinin (HA) and neuraminidase (NA). The valency of glycoconjugates was controlled by the reaction ratio of the S-sialoside monomer and protein. Hemagglutination inhibition assay showed that these synthetic glycoproteins have higher affinity to HA than the small clusters of sialosides with lower valency, due to multivalent effect and optimized three dimensional presentation of sialosides on the protein platform. The results of fluorescent NA inhibition assay showed that some of the conjugates have moderate NA inhibitory activity, in comparison to the monomer and low valent conjugates with weak or none inhibitory activity. These synthetic sialylated proteins were not cytotoxic with concentrations up to 100 μM, since the sialylation did not change the secondary structure of protein. This new kind of conjugates can be used as lead compounds for antiviral drug design and the construction of pseudo sialoside-protein conjugates library to investigate the carbohydrate-HA/NA recognition process and a platform for the influenza virus capturing.
Copyright ? 2016 Elsevier Ltd. All rights reserved.
[h=4]KEYWORDS:[/h] Antiviral inhibitor; Click chemistry; Glycoprotein; Multivalent effect
PMID: 27710815 DOI: 10.1016/j.carres.2016.09.017
[PubMed - as supplied by publisher]
[h=1]Multivalent S-sialoside protein conjugates block influenza hemagglutinin and neuraminidase.[/h] Yang Y[SUP]1[/SUP], Liu HP[SUP]2[/SUP], Yu Q[SUP]2[/SUP], Yang MB[SUP]2[/SUP], Wang DM[SUP]2[/SUP], Jia TW[SUP]2[/SUP], He HJ[SUP]2[/SUP], He Y[SUP]3[/SUP], Xiao HX[SUP]4[/SUP], Iyer SS[SUP]5[/SUP], Fan ZC[SUP]6[/SUP], Meng X[SUP]7[/SUP], Yu P[SUP]8[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] A new class of S-sialoside Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) conjugates were prepared to enhance the binding affinity to hemagglutinin (HA) and neuraminidase (NA). The valency of glycoconjugates was controlled by the reaction ratio of the S-sialoside monomer and protein. Hemagglutination inhibition assay showed that these synthetic glycoproteins have higher affinity to HA than the small clusters of sialosides with lower valency, due to multivalent effect and optimized three dimensional presentation of sialosides on the protein platform. The results of fluorescent NA inhibition assay showed that some of the conjugates have moderate NA inhibitory activity, in comparison to the monomer and low valent conjugates with weak or none inhibitory activity. These synthetic sialylated proteins were not cytotoxic with concentrations up to 100 μM, since the sialylation did not change the secondary structure of protein. This new kind of conjugates can be used as lead compounds for antiviral drug design and the construction of pseudo sialoside-protein conjugates library to investigate the carbohydrate-HA/NA recognition process and a platform for the influenza virus capturing.
Copyright ? 2016 Elsevier Ltd. All rights reserved.
[h=4]KEYWORDS:[/h] Antiviral inhibitor; Click chemistry; Glycoprotein; Multivalent effect
PMID: 27710815 DOI: 10.1016/j.carres.2016.09.017
[PubMed - as supplied by publisher]