tetano
Editor, Senior Moderator
Chem Commun (Camb). 2015 Jan 14. [Epub ahead of print]
[h=1]Understanding viral neuraminidase inhibition by substituted difluorosialic acids.[/h] Weck S[SUP]1[/SUP], Robinson K, Smith MR, Withers SG.
[h=3]Author information[/h]
[h=3]Abstract[/h] Mechanism-based inhibition of influenza neuraminidases by difluorosialic acids (DFSA) is not only rendered highly specific by incorporation of 4-amino or 4-guanidine substituents but also the half-life for reactivation is greatly increased. Measurement of rate constants for spontaneous hydrolysis of a series of such substituted DFSAs reveals, surprisingly, that inherent inductive effects play very little role in this rate reduction and that interactions with the enzyme are more important.
PMID: 25587931 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25587931
[h=1]Understanding viral neuraminidase inhibition by substituted difluorosialic acids.[/h] Weck S[SUP]1[/SUP], Robinson K, Smith MR, Withers SG.
[h=3]Author information[/h]
[h=3]Abstract[/h] Mechanism-based inhibition of influenza neuraminidases by difluorosialic acids (DFSA) is not only rendered highly specific by incorporation of 4-amino or 4-guanidine substituents but also the half-life for reactivation is greatly increased. Measurement of rate constants for spontaneous hydrolysis of a series of such substituted DFSAs reveals, surprisingly, that inherent inductive effects play very little role in this rate reduction and that interactions with the enzyme are more important.
PMID: 25587931 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25587931