tetano
Editor, Senior Moderator
Bioorg Med Chem Lett. 2014 Feb 18. pii: S0960-894X(14)00144-9. doi: 10.1016/j.bmcl.2014.02.021. [Epub ahead of print]
A phospha-oseltamivir-biotin conjugate as a strong and selective adhesive for the influenza virus.
Streicher H1, Martin SR2, Coombs PJ2, McCauley J3, Neill-Hall D4, Stanley M4.
Author information
Abstract
We present the synthesis and application of a molecule containing both the powerful influenza neuraminidase (NA) inhibitor phospha-oseltamivir and d-biotin, connected via an undecaethylene glycol spacer. It inhibits influenza virus neuraminidase (from the H3N2 X31 virus) in the same range as oseltamivir, with a slow off-rate, and produces a stable NA-coated surface when loaded onto streptavidin-coated biosensors. Purified X31 virus binds to these loaded biosensors with an apparent dissociation constant in the low picomolar range and binding of antibodies to the immobilized virus could be readily detected. The compound is thus a potential candidate for the selective immobilization of influenza virus in influenza diagnosis, vaccine choice, development or testing.
Copyright ? 2014 Elsevier Ltd. All rights reserved.
KEYWORDS:
Biosensors, Influenza virus, Neuraminidase inhibitor, Oseltamivir, Virus immobilisation
PMID:
24594352
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24594352
A phospha-oseltamivir-biotin conjugate as a strong and selective adhesive for the influenza virus.
Streicher H1, Martin SR2, Coombs PJ2, McCauley J3, Neill-Hall D4, Stanley M4.
Author information
Abstract
We present the synthesis and application of a molecule containing both the powerful influenza neuraminidase (NA) inhibitor phospha-oseltamivir and d-biotin, connected via an undecaethylene glycol spacer. It inhibits influenza virus neuraminidase (from the H3N2 X31 virus) in the same range as oseltamivir, with a slow off-rate, and produces a stable NA-coated surface when loaded onto streptavidin-coated biosensors. Purified X31 virus binds to these loaded biosensors with an apparent dissociation constant in the low picomolar range and binding of antibodies to the immobilized virus could be readily detected. The compound is thus a potential candidate for the selective immobilization of influenza virus in influenza diagnosis, vaccine choice, development or testing.
Copyright ? 2014 Elsevier Ltd. All rights reserved.
KEYWORDS:
Biosensors, Influenza virus, Neuraminidase inhibitor, Oseltamivir, Virus immobilisation
PMID:
24594352
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24594352