Haag R, et., al. Exploring rigid and flexible core trivalent sialosides for influenza virus inhibition. Chemistry. 2018 Oct 8.
We describe the chemical synthesis and binding analysis of functionalizable rigid and flexible core trivalent sialosides bearing oligoethylene glycol (OEG) spacers interacting with spike proteins of influenza A virus (IAV) X31. Although the flexible tris-based trivalent sialosides achieved micromolar binding constants, a trivalent binder based on a rigid adamantane core dominated flexible tripodal compounds with micromolar binding and hemagglutination inhibition constants. Simulation studies indicated increased conformational penalties for long OEG spacers. Using a systematic approach with molecular modeling and simulations as well as biophysical analysis, our findings emphasize on the importance of the scaffold rigidity and the challenges associated with the spacer length optimization.
See Also:
Latest articles in those days:
- Nucleic acid detection and genomic sequence analysis of one H5N1 avian influenza virus from wide birds around Qinghai Lake 1 days ago
- An aggregated dataset of serial morbidity and titer measurements from influenza A virus-infected ferrets 2 days ago
- Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation 4 days ago
- Risk assessment of a highly pathogenic H5N1 influenza virus from mink 4 days ago
- Detection of clade 2.3.4.4b highly pathogenic H5N1 influenza virus in New York City 4 days ago
[Go Top] [Close Window]